Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage (387 views visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1135-1142.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.605, 5-year impact factor Impact factor a 5 anni: 2.474
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-71749090850&partnerID=40&md5=6abbd805dd16f63a0563471ce03a0feb
Keywords Parole chiave: Crystal, Dna, Ribosome Inactivating Protein, Dna Cleavage, Double Strands, E. Coli, Functional Behaviors, Functional Changes, Glycosylated, Molecular Replacements, Phase Determination, Plasmid Pbr322, Ribosome-Inactivating Protein, Seeding Techniques, Structural Determinants, Two-Component, Escherichia Coli, Esterification, Fluorine Containing Polymers, Genes, Glycosylation, Nucleic Acids, Single Crystals, X Ray Crystallography, Crystal Structure, Protein Pd L1, Unclassified Drug, Vegetable Protein, Double Stranded Dna, Amino Acid Sequence, Article, Controlled Study, Nonhuman, Plant Leaf, Pokeweed, Protein Dna Interaction, Protein Expression, Protein Family, Protein Function, Protein Glycosylation, Protein Structure, Sequence Analysis, Binding Sites, X-Ray, Bacterial, Models, Molecular Sequence Data, Phytolacca, Plant Leaves, Plant Proteins, Protein Isoforms, Secondary, Tertiary, Recombinant Proteins, Type 1, Sequence Homology, Phytolacca Dioica,
Affiliations Affiliazioni:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli I-80134, Italy
Dipartimento di Scienze Della Vita, Seconda Università di Napoli, Via Vivaldi 43, Caserta I-81100, Italy
References Riferimenti:
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-68
Endo, Y., Tsurugi, K., (1987) J Biol Chem, 262, pp. 8128-8130
Endo, Y., Mitsui, K., Motizuki, M., Tsurugi, K., (1987) J Biol Chem, 262, pp. 5908-5912
Endo, Y., Chan, Y.L., Lin, A., Tsurugi, K., Wool, I.G., (1988) J Biol Chem, 263, pp. 7917-7920
Stirpe, F., Battelli, M.G., (2006) Cell Mol Life Sci, 63, pp. 1850-1866
Barbieri, L., Valbonesi, P., Bonora, E., Gorini, P., Bolognesi, A., Stirpe, F., (1997) Nucleic Acids Res, 25, pp. 518-522
Aceto, S., Di Maro, A., Conforto, B., Siniscalco, G.G., Parente, A., Delli Bovi, P., Gaudio, L., (2005) Biol Chem, 386, pp. 307-317
Bolognesi, A., Polito, L., Lubelli, C., Barbieri, L., Parente, A., Stirpe, F., (2002) J Biol Chem, 277, pp. 13709-13716
Mccluskey, A.J., Poon, G.M., Bolewska-Pedyczak, E., Srikumar, T., Jeram, S.M., Raught, B., Gariepy, J., (2008) J Mol Biol, 378, pp. 375-386
Chan, D.S., Chu, L.O., Lee, K.M., Too, P.H., Ma, K.W., Sze, K.H., Zhu, G., Wong, K.B., (2007) Nucleic Acids Res
Voss, C., Eyol, E., Frank, M., Von Der Lieth, C.W., Berger, M.R., (2006) FASEB J, 20, pp. 1194-1196
Schoffski, P., Riggert, S., Fumoleau, P., Campone, M., Bolte, O., Marreaud, S., Lacombe, D., Twelves, C., (2004) Ann Oncol, 15, pp. 1816-1824
Chu, K.T., Ng, T.B., (2006) Biochem Biophys Res Commun, 340, pp. 118-124
Wang, J.H., Nie, H.L., Tam, S.C., Huang, H., Zheng, Y.T., (2002) FEBS Lett, 531, pp. 295-298
Wang, Y.Y., Ouyang, D.Y., Huang, H., Chan, H., Tam, S.C., Zheng, Y.T., (2005) Biochem Biophys Res Commun, 331, pp. 1075-1080
Poyet, J.L., Hoeveler, A., Jongeneel, C.V., (1998) Biochem Biophys Res Commun, 253, pp. 582-587
Walker, D., Lancaster, L., James, R., Kleanthous, C., (2004) Protein Sci, 13, pp. 1603-1611
Mccullough, A.K., Sanchez, A., Dodson, M.L., Marapaka, P., Taylor, J.S., Lloyd, R.S., (2001) Biochemistry, 40, pp. 561-568
Robertus, J.D., Monzingo, A.F., (2004) Mini Rev Med Chem, 4, pp. 477-486
Day, P.J., Lord, J.M., Roberts, L.M., (1998) Eur J Biochem, 258, pp. 540-545
Ghosh, P., Batra, J.K., (2006) Biochem J, 400, pp. 99-104
Bagga, S., Seth, D., Batra, J.K., (2003) J Biol Chem, 278, pp. 4813-4820
Choudhary, N.L., Yadav, O.P., Lodha, M.L., (2008) Biochemistry, 73, pp. 273-277. , Mosc
Begam, M., Narwal, S., Roy, S., Kumar, S., Lodha, M.L., Kapoor, H.C., (2006) Biochemistry, 71 (SUPPL. 1), pp. S44-S48. , Mosc
Gasperi-Campani, A., Brognara, I., Baiocchi, D., Roncuzzi, L., (2005) Toxicon, 45, pp. 475-480
He, W.J., Liu, W.Y., (2004) Biochem J, 377, pp. 17-23
Brigotti, M., Carnicelli, D., Ravanelli, E., Vara, A.G., Martinelli, C., Alfieri, R.R., Petronini, P.G., Sestili, P., (2007) Infect Immun, 75, pp. 2201-2207
Wang, P., Tumer, N.E., (1999) Nucleic Acids Res, 27, pp. 1900-1905
Parente, A., Conforto, B., Di Maro, A., Chambery, A., De Luca, P., Bolognesi, A., Iriti, M., Faoro, F., (2008) Planta, 228, pp. 963-975
Di Maro, A., Valbonesi, P., Bolognesi, A., Stirpe, F., De Luca, P., Siniscalco Gigliano, G., Gaudio, L., Parente, A., (1999) Planta, 208, pp. 125-131
Chambery, A., Di Maro, A., Parente, A., (2008) Phytochemistry, 69, pp. 1973-1982
Esnouf, R.M., (1999) Acta Crystallogr D Biol Crystallogr, 55, pp. 938-940
Merritt, E.A., Bacon, D.J., (1997) Methods Enzymol, 277, pp. 505-524
Ruggiero, A., Chambery, A., Di Maro, A., Parente, A., Berisio, R., (2008) Proteins, 71, pp. 8-15
Kurinov, I.V., Myers, D.E., Irvin, J.D., Uckun, F.M., (1999) Protein Sci, 8, pp. 1765-1772
Ak, P., Benham, C.J., (2005) PLoS Comput Biol, 1, pp. e7
Benham, C.J., Bi, C., (2004) J Comput Biol, 11, pp. 519-543
Guo, Q., Zhou, W., Too, H.M., Li, J., Liu, Y., Bartlam, M., Dong, Y., Rao, Z., (2003) Protein Eng, 16, pp. 391-396
Nicolas, E., Beggs, J.M., Taraschi, T.F., (2000) J Biol Chem, 275, pp. 31399-31406
Yang, C.G., Yi, C., Duguid, E.M., Sullivan, C.T., Jian, X., Rice, P.A., He, C., (2008) Nature, 452, pp. 961-965
Wang, H., Kaloper, M., Benham, C.J., (2006) Nucl Acids Res, 34, pp. D373-D378
Vesnaver, G., Chang, C.N., Eisenberg, M., Grollman, A.P., Breslauer, K.J., (1989) Proc Natl Acad Sci USA, 86, pp. 3614-3618
Minor, W., Tomchick, D., Otwinowski, Z., (2000) Structure, 8, pp. R105-R110
Caliandro, R., Carrozzini, B., Cascarano, G.L., De Caro, L., Giacovazzo, C., Mazzone, A.M., Siliqi, D., (2006) J Appl Cryst, 39, pp. 185-193
Potterton, E., Briggs, P., Turkenburg, M., Dodson, E., (2003) Acta Crystallogr D Biol Crystallogr, 59, pp. 1131-1137
Murshudov, G.N., Vagin, A.A., Dodson, E.J., (1997) Acta Crystallogr D Biol Crystallogr, 53, pp. 240-255
Morris, R.J., Perrakis, A., Lamzin, V.S., (2003) Meth Enzymol, 374, pp. 229-244
Endo, Y., Chan, Y. L., Lin, A., Tsurugi, K., Wool, I. G., (1988) J Biol Chem, 263, pp. 7917-7920
Mccluskey, A. J., Poon, G. M., Bolewska-Pedyczak, E., Srikumar, T., Jeram, S. M., Raught, B., Gariepy, J., (2008) J Mol Biol, 378, pp. 375-386
Chan, D. S., Chu, L. O., Lee, K. M., Too, P. H., Ma, K. W., Sze, K. H., Zhu, G., Wong, K. B., (2007) Nucleic Acids Res
Chu, K. T., Ng, T. B., (2006) Biochem Biophys Res Commun, 340, pp. 118-124
Wang, J. H., Nie, H. L., Tam, S. C., Huang, H., Zheng, Y. T., (2002) FEBS Lett, 531, pp. 295-298
Wang, Y. Y., Ouyang, D. Y., Huang, H., Chan, H., Tam, S. C., Zheng, Y. T., (2005) Biochem Biophys Res Commun, 331, pp. 1075-1080
Poyet, J. L., Hoeveler, A., Jongeneel, C. V., (1998) Biochem Biophys Res Commun, 253, pp. 582-587
Mccullough, A. K., Sanchez, A., Dodson, M. L., Marapaka, P., Taylor, J. S., Lloyd, R. S., (2001) Biochemistry, 40, pp. 561-568
Robertus, J. D., Monzingo, A. F., (2004) Mini Rev Med Chem, 4, pp. 477-486
Day, P. J., Lord, J. M., Roberts, L. M., (1998) Eur J Biochem, 258, pp. 540-545
Choudhary, N. L., Yadav, O. P., Lodha, M. L., (2008) Biochemistry, 73, pp. 273-277. , Mosc
He, W. J., Liu, W. Y., (2004) Biochem J, 377, pp. 17-23
Wang, P., Tumer, N. E., (1999) Nucleic Acids Res, 27, pp. 1900-1905
Esnouf, R. M., (1999) Acta Crystallogr D Biol Crystallogr, 55, pp. 938-940
Merritt, E. A., Bacon, D. J., (1997) Methods Enzymol, 277, pp. 505-524
Kurinov, I. V., Myers, D. E., Irvin, J. D., Uckun, F. M., (1999) Protein Sci, 8, pp. 1765-1772
Ak, P., Benham, C. J., (2005) PLoS Comput Biol, 1, pp. e7
Benham, C. J., Bi, C., (2004) J Comput Biol, 11, pp. 519-543
Yang, C. G., Yi, C., Duguid, E. M., Sullivan, C. T., Jian, X., Rice, P. A., He, C., (2008) Nature, 452, pp. 961-965
Murshudov, G. N., Vagin, A. A., Dodson, E. J., (1997) Acta Crystallogr D Biol Crystallogr, 53, pp. 240-255
Morris, R. J., Perrakis, A., Lamzin, V. S., (2003) Meth Enzymol, 374, pp. 229-244
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1135-1142.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.605, 5-year impact factor Impact factor a 5 anni: 2.474
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-71749090850&partnerID=40&md5=6abbd805dd16f63a0563471ce03a0feb
Keywords Parole chiave: Crystal, Dna, Ribosome Inactivating Protein, Dna Cleavage, Double Strands, E. Coli, Functional Behaviors, Functional Changes, Glycosylated, Molecular Replacements, Phase Determination, Plasmid Pbr322, Ribosome-Inactivating Protein, Seeding Techniques, Structural Determinants, Two-Component, Escherichia Coli, Esterification, Fluorine Containing Polymers, Genes, Glycosylation, Nucleic Acids, Single Crystals, X Ray Crystallography, Crystal Structure, Protein Pd L1, Unclassified Drug, Vegetable Protein, Double Stranded Dna, Amino Acid Sequence, Article, Controlled Study, Nonhuman, Plant Leaf, Pokeweed, Protein Dna Interaction, Protein Expression, Protein Family, Protein Function, Protein Glycosylation, Protein Structure, Sequence Analysis, Binding Sites, X-Ray, Bacterial, Models, Molecular Sequence Data, Phytolacca, Plant Leaves, Plant Proteins, Protein Isoforms, Secondary, Tertiary, Recombinant Proteins, Type 1, Sequence Homology, Phytolacca Dioica,
Affiliations Affiliazioni:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli I-80134, Italy
Dipartimento di Scienze Della Vita, Seconda Università di Napoli, Via Vivaldi 43, Caserta I-81100, Italy
References Riferimenti:
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-68
Endo, Y., Tsurugi, K., (1987) J Biol Chem, 262, pp. 8128-8130
Endo, Y., Mitsui, K., Motizuki, M., Tsurugi, K., (1987) J Biol Chem, 262, pp. 5908-5912
Endo, Y., Chan, Y.L., Lin, A., Tsurugi, K., Wool, I.G., (1988) J Biol Chem, 263, pp. 7917-7920
Stirpe, F., Battelli, M.G., (2006) Cell Mol Life Sci, 63, pp. 1850-1866
Barbieri, L., Valbonesi, P., Bonora, E., Gorini, P., Bolognesi, A., Stirpe, F., (1997) Nucleic Acids Res, 25, pp. 518-522
Aceto, S., Di Maro, A., Conforto, B., Siniscalco, G.G., Parente, A., Delli Bovi, P., Gaudio, L., (2005) Biol Chem, 386, pp. 307-317
Bolognesi, A., Polito, L., Lubelli, C., Barbieri, L., Parente, A., Stirpe, F., (2002) J Biol Chem, 277, pp. 13709-13716
Mccluskey, A.J., Poon, G.M., Bolewska-Pedyczak, E., Srikumar, T., Jeram, S.M., Raught, B., Gariepy, J., (2008) J Mol Biol, 378, pp. 375-386
Chan, D.S., Chu, L.O., Lee, K.M., Too, P.H., Ma, K.W., Sze, K.H., Zhu, G., Wong, K.B., (2007) Nucleic Acids Res
Voss, C., Eyol, E., Frank, M., Von Der Lieth, C.W., Berger, M.R., (2006) FASEB J, 20, pp. 1194-1196
Schoffski, P., Riggert, S., Fumoleau, P., Campone, M., Bolte, O., Marreaud, S., Lacombe, D., Twelves, C., (2004) Ann Oncol, 15, pp. 1816-1824
Chu, K.T., Ng, T.B., (2006) Biochem Biophys Res Commun, 340, pp. 118-124
Wang, J.H., Nie, H.L., Tam, S.C., Huang, H., Zheng, Y.T., (2002) FEBS Lett, 531, pp. 295-298
Wang, Y.Y., Ouyang, D.Y., Huang, H., Chan, H., Tam, S.C., Zheng, Y.T., (2005) Biochem Biophys Res Commun, 331, pp. 1075-1080
Poyet, J.L., Hoeveler, A., Jongeneel, C.V., (1998) Biochem Biophys Res Commun, 253, pp. 582-587
Walker, D., Lancaster, L., James, R., Kleanthous, C., (2004) Protein Sci, 13, pp. 1603-1611
Mccullough, A.K., Sanchez, A., Dodson, M.L., Marapaka, P., Taylor, J.S., Lloyd, R.S., (2001) Biochemistry, 40, pp. 561-568
Robertus, J.D., Monzingo, A.F., (2004) Mini Rev Med Chem, 4, pp. 477-486
Day, P.J., Lord, J.M., Roberts, L.M., (1998) Eur J Biochem, 258, pp. 540-545
Ghosh, P., Batra, J.K., (2006) Biochem J, 400, pp. 99-104
Bagga, S., Seth, D., Batra, J.K., (2003) J Biol Chem, 278, pp. 4813-4820
Choudhary, N.L., Yadav, O.P., Lodha, M.L., (2008) Biochemistry, 73, pp. 273-277. , Mosc
Begam, M., Narwal, S., Roy, S., Kumar, S., Lodha, M.L., Kapoor, H.C., (2006) Biochemistry, 71 (SUPPL. 1), pp. S44-S48. , Mosc
Gasperi-Campani, A., Brognara, I., Baiocchi, D., Roncuzzi, L., (2005) Toxicon, 45, pp. 475-480
He, W.J., Liu, W.Y., (2004) Biochem J, 377, pp. 17-23
Brigotti, M., Carnicelli, D., Ravanelli, E., Vara, A.G., Martinelli, C., Alfieri, R.R., Petronini, P.G., Sestili, P., (2007) Infect Immun, 75, pp. 2201-2207
Wang, P., Tumer, N.E., (1999) Nucleic Acids Res, 27, pp. 1900-1905
Parente, A., Conforto, B., Di Maro, A., Chambery, A., De Luca, P., Bolognesi, A., Iriti, M., Faoro, F., (2008) Planta, 228, pp. 963-975
Di Maro, A., Valbonesi, P., Bolognesi, A., Stirpe, F., De Luca, P., Siniscalco Gigliano, G., Gaudio, L., Parente, A., (1999) Planta, 208, pp. 125-131
Chambery, A., Di Maro, A., Parente, A., (2008) Phytochemistry, 69, pp. 1973-1982
Esnouf, R.M., (1999) Acta Crystallogr D Biol Crystallogr, 55, pp. 938-940
Merritt, E.A., Bacon, D.J., (1997) Methods Enzymol, 277, pp. 505-524
Ruggiero, A., Chambery, A., Di Maro, A., Parente, A., Berisio, R., (2008) Proteins, 71, pp. 8-15
Kurinov, I.V., Myers, D.E., Irvin, J.D., Uckun, F.M., (1999) Protein Sci, 8, pp. 1765-1772
Ak, P., Benham, C.J., (2005) PLoS Comput Biol, 1, pp. e7
Benham, C.J., Bi, C., (2004) J Comput Biol, 11, pp. 519-543
Guo, Q., Zhou, W., Too, H.M., Li, J., Liu, Y., Bartlam, M., Dong, Y., Rao, Z., (2003) Protein Eng, 16, pp. 391-396
Nicolas, E., Beggs, J.M., Taraschi, T.F., (2000) J Biol Chem, 275, pp. 31399-31406
Yang, C.G., Yi, C., Duguid, E.M., Sullivan, C.T., Jian, X., Rice, P.A., He, C., (2008) Nature, 452, pp. 961-965
Wang, H., Kaloper, M., Benham, C.J., (2006) Nucl Acids Res, 34, pp. D373-D378
Vesnaver, G., Chang, C.N., Eisenberg, M., Grollman, A.P., Breslauer, K.J., (1989) Proc Natl Acad Sci USA, 86, pp. 3614-3618
Minor, W., Tomchick, D., Otwinowski, Z., (2000) Structure, 8, pp. R105-R110
Caliandro, R., Carrozzini, B., Cascarano, G.L., De Caro, L., Giacovazzo, C., Mazzone, A.M., Siliqi, D., (2006) J Appl Cryst, 39, pp. 185-193
Potterton, E., Briggs, P., Turkenburg, M., Dodson, E., (2003) Acta Crystallogr D Biol Crystallogr, 59, pp. 1131-1137
Murshudov, G.N., Vagin, A.A., Dodson, E.J., (1997) Acta Crystallogr D Biol Crystallogr, 53, pp. 240-255
Morris, R.J., Perrakis, A., Lamzin, V.S., (2003) Meth Enzymol, 374, pp. 229-244
Endo, Y., Chan, Y. L., Lin, A., Tsurugi, K., Wool, I. G., (1988) J Biol Chem, 263, pp. 7917-7920
Mccluskey, A. J., Poon, G. M., Bolewska-Pedyczak, E., Srikumar, T., Jeram, S. M., Raught, B., Gariepy, J., (2008) J Mol Biol, 378, pp. 375-386
Chan, D. S., Chu, L. O., Lee, K. M., Too, P. H., Ma, K. W., Sze, K. H., Zhu, G., Wong, K. B., (2007) Nucleic Acids Res
Chu, K. T., Ng, T. B., (2006) Biochem Biophys Res Commun, 340, pp. 118-124
Wang, J. H., Nie, H. L., Tam, S. C., Huang, H., Zheng, Y. T., (2002) FEBS Lett, 531, pp. 295-298
Wang, Y. Y., Ouyang, D. Y., Huang, H., Chan, H., Tam, S. C., Zheng, Y. T., (2005) Biochem Biophys Res Commun, 331, pp. 1075-1080
Poyet, J. L., Hoeveler, A., Jongeneel, C. V., (1998) Biochem Biophys Res Commun, 253, pp. 582-587
Mccullough, A. K., Sanchez, A., Dodson, M. L., Marapaka, P., Taylor, J. S., Lloyd, R. S., (2001) Biochemistry, 40, pp. 561-568
Robertus, J. D., Monzingo, A. F., (2004) Mini Rev Med Chem, 4, pp. 477-486
Day, P. J., Lord, J. M., Roberts, L. M., (1998) Eur J Biochem, 258, pp. 540-545
Choudhary, N. L., Yadav, O. P., Lodha, M. L., (2008) Biochemistry, 73, pp. 273-277. , Mosc
He, W. J., Liu, W. Y., (2004) Biochem J, 377, pp. 17-23
Wang, P., Tumer, N. E., (1999) Nucleic Acids Res, 27, pp. 1900-1905
Esnouf, R. M., (1999) Acta Crystallogr D Biol Crystallogr, 55, pp. 938-940
Merritt, E. A., Bacon, D. J., (1997) Methods Enzymol, 277, pp. 505-524
Kurinov, I. V., Myers, D. E., Irvin, J. D., Uckun, F. M., (1999) Protein Sci, 8, pp. 1765-1772
Ak, P., Benham, C. J., (2005) PLoS Comput Biol, 1, pp. e7
Benham, C. J., Bi, C., (2004) J Comput Biol, 11, pp. 519-543
Yang, C. G., Yi, C., Duguid, E. M., Sullivan, C. T., Jian, X., Rice, P. A., He, C., (2008) Nature, 452, pp. 961-965
Murshudov, G. N., Vagin, A. A., Dodson, E. J., (1997) Acta Crystallogr D Biol Crystallogr, 53, pp. 240-255
Morris, R. J., Perrakis, A., Lamzin, V. S., (2003) Meth Enzymol, 374, pp. 229-244
Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage
The structure of the highly glycosylated type 1 ribosome inactivating protein PD-L1 was determined by X-ray crystallography. This protein belongs to a group of four PD-Ls (PD-L1-4) expressed in Phytolacca dioica leaves. Of these, PD-L1 and PD-L2 are endowed with the ability to cleave double strand DNA, a property which is not shared by the other two components of the family. Single crystals of native PD-L1, the most glycosylated, were obtained using seeding techniques and phase determination was achieved using molecular replacement. To investigate the role of glycosylation in the different functionality of these proteins, we performed DNA cleavage assays on the E. coli plasmid pBR322. These experiments revealed that DNA cleaving ability does not depend on the level of glycosylation of PD-L1, since there is no difference in the activities displayed by native PD-L1 and a recombinant non-glycosylated form. Besides, confirming that DNA cleavage by PD-L1 cannot be attributed to contaminations, these data unambiguously show that functional changes between PD-L1 and PD-L4 are solely to be attributed to their sequence differences. On the basis of the comparison of PD-L1 and PD-L4 crystal structures, we propose possible structural determinants responsible for their different functional behavior. © 2009 Wiley Periodicals, Inc.
The structure of the highly glycosylated type 1 ribosome inactivating protein PD-L1 was determined by X-ray crystallography. This protein belongs to a group of four PD-Ls (PD-L1-4) expressed in Phytolacca dioica leaves. Of these, PD-L1 and PD-L2 are endowed with the ability to cleave double strand DNA, a property which is not shared by the other two components of the family. Single crystals of native PD-L1, the most glycosylated, were obtained using seeding techniques and phase determination was achieved using molecular replacement. To investigate the role of glycosylation in the different functionality of these proteins, we performed DNA cleavage assays on the E. coli plasmid pBR322. These experiments revealed that DNA cleaving ability does not depend on the level of glycosylation of PD-L1, since there is no difference in the activities displayed by native PD-L1 and a recombinant non-glycosylated form. Besides, confirming that DNA cleavage by PD-L1 cannot be attributed to contaminations, these data unambiguously show that functional changes between PD-L1 and PD-L4 are solely to be attributed to their sequence differences. On the basis of the comparison of PD-L1 and PD-L4 crystal structures, we propose possible structural determinants responsible for their different functional behavior. © 2009 Wiley Periodicals, Inc.
Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage
No results. Nessun risultato. |
Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage
Di Maro A, Berisio R, Ruggiero A, Tamburino R, Severino V, Zacchia E, Parente A
* Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica (332 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 May 11; 421(3): 514-520.
Impact Factor: 2.406
Dettagli Esporta in BibTeX Esporta in EndNote
Parente A, Berisio R, Chambery A, Di Maro A
* Ribosome Inactivating Proteins from P. dioica leaves (191 visite)
Springer Eds, 2010; N/D: N/D-N/D.
Impact Factor: 0
Dettagli Esporta in BibTeX Esporta in EndNote
Severino V, Chambery A, Di Maro A, Marasco D, Ruggiero A, Berisio R, Giansanti F, Ippoliti R, Parente A
* The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves (358 visite)
Mol Biosyst (ISSN: 1742-206x), 2010; 6(3): 570-579.
Impact Factor: 3.825
Dettagli Esporta in BibTeX Esporta in EndNote
Santoro F, Barone V, Improta R
* The Excited States Decay Of The A-T Dna: A Pcm/Td-Dft Study In Aqueous Solution Of The (9-Methyl-Adenine) 2 (1-Methyl-Thymine) 2 Stacked Tetramer (226 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(42): 15232-15245.
Impact Factor: 8.58
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Parente A, Berisio R
* Atomic Resolution (1. 1 Angstrom) Structure Of The Ribosome-Inactivating Protein Pd-L4 From Phytolacca Dioica L. Leaves (350 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Apr; 71(1): 8-15.
Impact Factor: 3.419
Dettagli Esporta in BibTeX Esporta in EndNote
Chambery A, Pisante M, Di Maro A, Di Zazzo E, Ruvo M, Costantini S, Colonna G, Parente A
* Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (328 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Impact Factor: 3.354
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Mastroianni A, Parente A, Berisio R
* Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity (277 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2007; 14(4): 407-409.
Impact Factor: 1.097
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Pisante M, Parente A, Berisio R
* Crystallization and preliminary x-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves (340 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2007; 14(1): 97-100.
Impact Factor: 1.097
Dettagli Esporta in BibTeX Esporta in EndNote
8 Records (8 escludendo Abstract e Conferenze).
Impact factor totale: 23.778 (23.778 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 25.253 (25.253 escludendo Abstract e Conferenze).
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Di Maro A, Berisio R, Ruggiero A, Tamburino R, Severino V, Zacchia E, Parente A
* Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica (332 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 May 11; 421(3): 514-520.
Impact Factor: 2.406
Dettagli Esporta in BibTeX Esporta in EndNote
Parente A, Berisio R, Chambery A, Di Maro A
* Ribosome Inactivating Proteins from P. dioica leaves (191 visite)
Springer Eds, 2010; N/D: N/D-N/D.
Impact Factor: 0
Dettagli Esporta in BibTeX Esporta in EndNote
Severino V, Chambery A, Di Maro A, Marasco D, Ruggiero A, Berisio R, Giansanti F, Ippoliti R, Parente A
* The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves (358 visite)
Mol Biosyst (ISSN: 1742-206x), 2010; 6(3): 570-579.
Impact Factor: 3.825
Dettagli Esporta in BibTeX Esporta in EndNote
Santoro F, Barone V, Improta R
* The Excited States Decay Of The A-T Dna: A Pcm/Td-Dft Study In Aqueous Solution Of The (9-Methyl-Adenine) 2 (1-Methyl-Thymine) 2 Stacked Tetramer (226 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(42): 15232-15245.
Impact Factor: 8.58
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Parente A, Berisio R
* Atomic Resolution (1. 1 Angstrom) Structure Of The Ribosome-Inactivating Protein Pd-L4 From Phytolacca Dioica L. Leaves (350 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Apr; 71(1): 8-15.
Impact Factor: 3.419
Dettagli Esporta in BibTeX Esporta in EndNote
Chambery A, Pisante M, Di Maro A, Di Zazzo E, Ruvo M, Costantini S, Colonna G, Parente A
* Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (328 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Impact Factor: 3.354
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Mastroianni A, Parente A, Berisio R
* Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity (277 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2007; 14(4): 407-409.
Impact Factor: 1.097
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Chambery A, Di Maro A, Pisante M, Parente A, Berisio R
* Crystallization and preliminary x-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves (340 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2007; 14(1): 97-100.
Impact Factor: 1.097
Dettagli Esporta in BibTeX Esporta in EndNote
8 Records (8 escludendo Abstract e Conferenze).
Impact factor totale: 23.778 (23.778 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 25.253 (25.253 escludendo Abstract e Conferenze).
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