Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (312 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.843, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2542445275&partnerID=40&md5=029e1fe19a34de7c999989e8cc70b569
Keywords: Antibiotics Synergism, Azithromycin, Dual Binding, Peptide-Bond Formation, Positional Catalysis, Ribosome, Synercid, Amino Acid, Antibiotic Agent, Chloramphenicol, Dalfopristin Plus Quinupristin, Macrolide, Messenger Rna, Nucleotide, Streptogramin, Transfer Rna, Troleandomycin, Untranslated Region, Accuracy, Chirality, Conference Paper, Crystallography, Drug Binding, Drug Potentiation, Molecular Interaction, Nonhuman, Polymerization, Priority Journal, Protein Interaction, Protein Synthesis, Rna Transport, Rotation, Anti-Bacterial Agents, X-Ray, Models, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Substrate Specificity, Virginiamycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Naples, Italy
References:
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Yonath, A., (2000) Cell, 102, pp. 615-62
Wimberly, B.T., Brodersen, D.E., Clemons Jr., W.M., Morgan-Warren, R.J., Carter, A.P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Cate, J.H., Noller, H.F., (2001) Science, 292, pp. 883-896
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-688
Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., (2000) Science, 289, pp. 905-920
Schmeing, T.M., Seila, A.C., Hansen, J.L., Freeborn, B., Soukup, J.K., Scaringe, S.A., Strobel, S.A., Steitz, T.A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J.L., Ippolito, J.A., Ban, N., Nissen, P., Moore, P.B., Steitz, T.A., (2002) Mol. Cell, 10, pp. 117-128
Hansen, J.L., Schmeing, T.M., Moore, P.B., Steitz, T.A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., (2003) Mol. Cell., 11, pp. 91-102
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., (2003) Nat. Struct. Biol., 10, pp. 366-370
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A.S., Fucini, P., Yonath, A., (2003) J. Bacteriol., 185, pp. 4276-4279
Harms, J.M., Schluenzen, F., Fucini, Bartels, H., Yonath, A., (2004) BMC Biol., , (in press)
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., (2003) Eur. J. Biochem., 270, pp. 2543-2556
Agmon, I., Bashan, A., Zarivach, R., Yonath, A., (2004), submittedMoore, P.B., Steitz, T.A., (2003) RNA, 9, pp. 155-159
Yonath, A., (2003) Chem. Biol. Chem., 4, pp. 1008-1017
Samaha, R.R., Green, R., Noller, H.F., (1995) Nature, 377, pp. 309-314
Fujiwara, S., Lee, S.G., Haruki, M., Kanaya, S., Takagi, M., Imanaka, T., (1996) FEBS Lett., 394, pp. 66-70
Uhlein, M., Weglohner, W., Urlaub, H., Wittmann-Liebold, B., (1998) Biochem. J., 331, pp. 423-430
Nitta, I., Kamada, Y., Noda, H., Ueda, T., Watanabe, K., (1998) Science, 281, pp. 666-669
Kim, D.F., Green, R., (1999) Mol. Cell., 4, pp. 859-864
Miskin, R., Zamir, A., Elson, D., (1968) Biochem. Biophys. Res. Commun., 33, pp. 551-557
Vogel, Z., Vogel, T., Zamir, A., Elson, D., (1971) J. Mol. Biol., 60, pp. 339-346
Zamir, A., Miskin, R., Vogel, Z., Elson, D., (1974) Methods Enzymol., 30, pp. 406-426
Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Yonath, A., (2002) Annu. Rev. Biophys. Biomol. Struct., 31, pp. 257-273
Dedkova, L.M., Fahmi, N.E., Golovine, S.Y., Hecht, S.M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Green, R., Samaha, R.R., Noller, H.F., (1997) J. Mol. Biol., 266, pp. 40-50
Wower, J., Kirillov, S.V., Wower, I.K., Guven, S., Hixson, S.S., Zimmermann, R.A., (2000) J. Biol. Chem., 275, pp. 37887-37894
Bocchetta, M., Xiong, L., Mankin, A.S., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 3525-3530
Porse, B.T., Thi-Ngoc, H.P., Garrett, R.A., (1996) J. Mol. Biol., 264, pp. 472-483
Moazed, D., Noller, H.F., (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 3725-3728
Auerbach, T., Bashan, A., Harms, J., Schluenzen, F., Zarivach, R., Bartels, H., Agmon, I., Yonath, A., (2002) Curr. Drug Targets - Infect. Disord., 2, pp. 169-186
Cocito, C., Di Giambattista, M., Nyssen, E., Vannuffel, P., (1997) J. Antimicrob. Chemother., 39, pp. 7-13
Allignet, J., Aubert, S., Morvan, A., El Solh, N., (1996) Antimicrob. Agents Chemother., 40, pp. 2523-2528
Malbruny, B., Canu, A., Bozdogan, B., Fantin, B., Zarrouk, V., Dutka-Malen, S., Feger, C., Leclercq, R., (2002) Antimicrob. Agents Chemother., 46, pp. 2200-2207
Nyssen, E., Di Giambattista, M., Cocito, C., (1989) Biochim. Biophys. Acta, 1009, pp. 39-46
Parfait, R., Cocito, C., (1980) Proc. Natl. Acad. Sci. USA, 77, pp. 5492-5496
Nakashio, S., Iwasawa, H., Iino, S., Shimada, J., (1997) Jpn. J. Antibiot., 50, pp. 844-853
Parfait, R., Di Giambattista, M., Cocito, C., (1981) Biochim. Biophys. Acta, 654, pp. 236-241
Pereyre, S., Gonzalez, P., De Barbeyrac, B., Darnige, A., Renaudin, H., Charron, A., Raherison, S., Bebear, C.M., (2002) Antimicrob. Agents Chemother., 46, pp. 3142-3150
Chinali, G., Moureau, P., Cocito, C.G., (1984) J. Biol. Chem., 259, pp. 9563-9568
Porse, B.T., Garrett, R.A., (1999) J. Mol. Biol., 286, pp. 375-387
Rodriguez-Fonseca, C., Amils, R., Garrett, R.A., (1995) J. Mol. Biol., 247, pp. 224-235
Hansen, J.L., Moore, P.B., Steitz, T.A., (2003) J. Mol. Biol., 330, pp. 1061-1075
Porse, B.T., Kirillov, S.V., Awayez, M.J., Garrett, R.A., (1999) RNA, 5, pp. 585-595
Bright, G.M., Nagel, A.A., Bordner, J., Desai, K.A., Dibrino, J.N., Nowakowska, J., Vincent, L., English, A.R., (1988) J. Antibiot., 41, pp. 1029-1047
Wittmann, H.G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., (1973) Mol. Gen. Genet., 127, pp. 175-189
Wimberly, B. T., Brodersen, D. E., Clemons Jr., W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H., Noller, H. F., (2001) Science, 292, pp. 883-896
Schmeing, T. M., Seila, A. C., Hansen, J. L., Freeborn, B., Soukup, J. K., Scaringe, S. A., Strobel, S. A., Steitz, T. A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J. L., Ippolito, J. A., Ban, N., Nissen, P., Moore, P. B., Steitz, T. A., (2002) Mol. Cell, 10, pp. 117-128
Hansen, J. L., Schmeing, T. M., Moore, P. B., Steitz, T. A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Harms, J. M., Schluenzen, F., Fucini, Bartels, H., Yonath, A., (2004) BMC Biol., , (in press)
Samaha, R. R., Green, R., Noller, H. F., (1995) Nature, 377, pp. 309-314
Kim, D. F., Green, R., (1999) Mol. Cell., 4, pp. 859-864
Bayfield, M. A., Dahlberg, A. E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Dedkova, L. M., Fahmi, N. E., Golovine, S. Y., Hecht, S. M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Porse, B. T., Thi-Ngoc, H. P., Garrett, R. A., (1996) J. Mol. Biol., 264, pp. 472-483
Porse, B. T., Garrett, R. A., (1999) J. Mol. Biol., 286, pp. 375-387
Hansen, J. L., Moore, P. B., Steitz, T. A., (2003) J. Mol. Biol., 330, pp. 1061-1075
Porse, B. T., Kirillov, S. V., Awayez, M. J., Garrett, R. A., (1999) RNA, 5, pp. 585-595
Bright, G. M., Nagel, A. A., Bordner, J., Desai, K. A., Dibrino, J. N., Nowakowska, J., Vincent, L., English, A. R., (1988) J. Antibiot., 41, pp. 1029-1047
Wittmann, H. G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., (1973) Mol. Gen. Genet., 127, pp. 175-189
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.843, 5-year impact factor: 3.47
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2542445275&partnerID=40&md5=029e1fe19a34de7c999989e8cc70b569
Keywords: Antibiotics Synergism, Azithromycin, Dual Binding, Peptide-Bond Formation, Positional Catalysis, Ribosome, Synercid, Amino Acid, Antibiotic Agent, Chloramphenicol, Dalfopristin Plus Quinupristin, Macrolide, Messenger Rna, Nucleotide, Streptogramin, Transfer Rna, Troleandomycin, Untranslated Region, Accuracy, Chirality, Conference Paper, Crystallography, Drug Binding, Drug Potentiation, Molecular Interaction, Nonhuman, Polymerization, Priority Journal, Protein Interaction, Protein Synthesis, Rna Transport, Rotation, Anti-Bacterial Agents, X-Ray, Models, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Substrate Specificity, Virginiamycin,
Affiliations:
*** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. Ribosomal Struct., 22603 Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, 80138 Naples, Italy
References:
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Yonath, A., (2000) Cell, 102, pp. 615-62
Wimberly, B.T., Brodersen, D.E., Clemons Jr., W.M., Morgan-Warren, R.J., Carter, A.P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M.M., Yusupova, G.Z., Baucom, A., Lieberman, K., Earnest, T.N., Cate, J.H., Noller, H.F., (2001) Science, 292, pp. 883-896
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Yonath, A., (2001) Cell, 107, pp. 679-688
Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A., (2000) Science, 289, pp. 905-920
Schmeing, T.M., Seila, A.C., Hansen, J.L., Freeborn, B., Soukup, J.K., Scaringe, S.A., Strobel, S.A., Steitz, T.A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J.L., Ippolito, J.A., Ban, N., Nissen, P., Moore, P.B., Steitz, T.A., (2002) Mol. Cell, 10, pp. 117-128
Hansen, J.L., Schmeing, T.M., Moore, P.B., Steitz, T.A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Yonath, A., (2003) Mol. Cell., 11, pp. 91-102
Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., Yonath, A., (2003) Nat. Struct. Biol., 10, pp. 366-370
Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A.S., Fucini, P., Yonath, A., (2003) J. Bacteriol., 185, pp. 4276-4279
Harms, J.M., Schluenzen, F., Fucini, Bartels, H., Yonath, A., (2004) BMC Biol., , (in press)
Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Yonath, A., (2003) Biopolymers, 70, pp. 19-41
Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Zarivach, R., (2003) Eur. J. Biochem., 270, pp. 2543-2556
Agmon, I., Bashan, A., Zarivach, R., Yonath, A., (2004), submittedMoore, P.B., Steitz, T.A., (2003) RNA, 9, pp. 155-159
Yonath, A., (2003) Chem. Biol. Chem., 4, pp. 1008-1017
Samaha, R.R., Green, R., Noller, H.F., (1995) Nature, 377, pp. 309-314
Fujiwara, S., Lee, S.G., Haruki, M., Kanaya, S., Takagi, M., Imanaka, T., (1996) FEBS Lett., 394, pp. 66-70
Uhlein, M., Weglohner, W., Urlaub, H., Wittmann-Liebold, B., (1998) Biochem. J., 331, pp. 423-430
Nitta, I., Kamada, Y., Noda, H., Ueda, T., Watanabe, K., (1998) Science, 281, pp. 666-669
Kim, D.F., Green, R., (1999) Mol. Cell., 4, pp. 859-864
Miskin, R., Zamir, A., Elson, D., (1968) Biochem. Biophys. Res. Commun., 33, pp. 551-557
Vogel, Z., Vogel, T., Zamir, A., Elson, D., (1971) J. Mol. Biol., 60, pp. 339-346
Zamir, A., Miskin, R., Vogel, Z., Elson, D., (1974) Methods Enzymol., 30, pp. 406-426
Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Yonath, A., (2002) Annu. Rev. Biophys. Biomol. Struct., 31, pp. 257-273
Dedkova, L.M., Fahmi, N.E., Golovine, S.Y., Hecht, S.M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Green, R., Samaha, R.R., Noller, H.F., (1997) J. Mol. Biol., 266, pp. 40-50
Wower, J., Kirillov, S.V., Wower, I.K., Guven, S., Hixson, S.S., Zimmermann, R.A., (2000) J. Biol. Chem., 275, pp. 37887-37894
Bocchetta, M., Xiong, L., Mankin, A.S., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 3525-3530
Porse, B.T., Thi-Ngoc, H.P., Garrett, R.A., (1996) J. Mol. Biol., 264, pp. 472-483
Moazed, D., Noller, H.F., (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 3725-3728
Auerbach, T., Bashan, A., Harms, J., Schluenzen, F., Zarivach, R., Bartels, H., Agmon, I., Yonath, A., (2002) Curr. Drug Targets - Infect. Disord., 2, pp. 169-186
Cocito, C., Di Giambattista, M., Nyssen, E., Vannuffel, P., (1997) J. Antimicrob. Chemother., 39, pp. 7-13
Allignet, J., Aubert, S., Morvan, A., El Solh, N., (1996) Antimicrob. Agents Chemother., 40, pp. 2523-2528
Malbruny, B., Canu, A., Bozdogan, B., Fantin, B., Zarrouk, V., Dutka-Malen, S., Feger, C., Leclercq, R., (2002) Antimicrob. Agents Chemother., 46, pp. 2200-2207
Nyssen, E., Di Giambattista, M., Cocito, C., (1989) Biochim. Biophys. Acta, 1009, pp. 39-46
Parfait, R., Cocito, C., (1980) Proc. Natl. Acad. Sci. USA, 77, pp. 5492-5496
Nakashio, S., Iwasawa, H., Iino, S., Shimada, J., (1997) Jpn. J. Antibiot., 50, pp. 844-853
Parfait, R., Di Giambattista, M., Cocito, C., (1981) Biochim. Biophys. Acta, 654, pp. 236-241
Pereyre, S., Gonzalez, P., De Barbeyrac, B., Darnige, A., Renaudin, H., Charron, A., Raherison, S., Bebear, C.M., (2002) Antimicrob. Agents Chemother., 46, pp. 3142-3150
Chinali, G., Moureau, P., Cocito, C.G., (1984) J. Biol. Chem., 259, pp. 9563-9568
Porse, B.T., Garrett, R.A., (1999) J. Mol. Biol., 286, pp. 375-387
Rodriguez-Fonseca, C., Amils, R., Garrett, R.A., (1995) J. Mol. Biol., 247, pp. 224-235
Hansen, J.L., Moore, P.B., Steitz, T.A., (2003) J. Mol. Biol., 330, pp. 1061-1075
Porse, B.T., Kirillov, S.V., Awayez, M.J., Garrett, R.A., (1999) RNA, 5, pp. 585-595
Bright, G.M., Nagel, A.A., Bordner, J., Desai, K.A., Dibrino, J.N., Nowakowska, J., Vincent, L., English, A.R., (1988) J. Antibiot., 41, pp. 1029-1047
Wittmann, H.G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., (1973) Mol. Gen. Genet., 127, pp. 175-189
Wimberly, B. T., Brodersen, D. E., Clemons Jr., W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., Ramakrishnan, V., (2000) Nature, 407, pp. 327-339
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H., Noller, H. F., (2001) Science, 292, pp. 883-896
Schmeing, T. M., Seila, A. C., Hansen, J. L., Freeborn, B., Soukup, J. K., Scaringe, S. A., Strobel, S. A., Steitz, T. A., (2002) Nat. Struct. Biol., 9, pp. 225-230
Hansen, J. L., Ippolito, J. A., Ban, N., Nissen, P., Moore, P. B., Steitz, T. A., (2002) Mol. Cell, 10, pp. 117-128
Hansen, J. L., Schmeing, T. M., Moore, P. B., Steitz, T. A., (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 11670-11675
Harms, J. M., Schluenzen, F., Fucini, Bartels, H., Yonath, A., (2004) BMC Biol., , (in press)
Samaha, R. R., Green, R., Noller, H. F., (1995) Nature, 377, pp. 309-314
Kim, D. F., Green, R., (1999) Mol. Cell., 4, pp. 859-864
Bayfield, M. A., Dahlberg, A. E., Schulmeister, U., Dorner, S., Barta, A., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 10096-10101
Dedkova, L. M., Fahmi, N. E., Golovine, S. Y., Hecht, S. M., (2003) J. Am. Chem. Soc., 125, pp. 6616-6617
Porse, B. T., Thi-Ngoc, H. P., Garrett, R. A., (1996) J. Mol. Biol., 264, pp. 472-483
Porse, B. T., Garrett, R. A., (1999) J. Mol. Biol., 286, pp. 375-387
Hansen, J. L., Moore, P. B., Steitz, T. A., (2003) J. Mol. Biol., 330, pp. 1061-1075
Porse, B. T., Kirillov, S. V., Awayez, M. J., Garrett, R. A., (1999) RNA, 5, pp. 585-595
Bright, G. M., Nagel, A. A., Bordner, J., Desai, K. A., Dibrino, J. N., Nowakowska, J., Vincent, L., English, A. R., (1988) J. Antibiot., 41, pp. 1029-1047
Wittmann, H. G., Stoffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Otaka, E., (1973) Mol. Gen. Genet., 127, pp. 175-189
Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3′end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3′end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
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Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
Other filter: ([btitle,keywords] "Antibiotics Synergis ...
Zarivach R, Bashan A, Berisio R, Harms J, Auerbach T, Schluenzen F, Bartels H, Baram D, Pyetan E, Sittner A, Amit M, Hansen HAS, Kessler M, Liebe C, Wolff A, Agmon I, Yonath A
* Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (490 views)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Impact Factor: 1.211
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (603 views)
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Impact Factor: 2.733
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (379 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
View Export to BibTeX Export to EndNote
* Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (490 views)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Impact Factor: 1.211
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (603 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (379 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
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3 Records (3 excluding Abstracts).
Total impact factor: 15.523 (15.523 excluding Abstracts).
Total 5 year impact factor: 17.085 (17.085 excluding Abstracts).
Total impact factor: 15.523 (15.523 excluding Abstracts).
Total 5 year impact factor: 17.085 (17.085 excluding Abstracts).
312 views. Last view on Thursday 09 March 2023, 9:54:56
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