Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteins
Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteins(470 views) Di Fiore A, Fiorentino G, Vitale RM, Ronca R, Amodeo P, Pedone C, Bartolucci S, De Simone G
Keywords: Archaea, Crystal Structure, Marr Family, Targeted Molecular Dynamics Simulation, Transcriptional Activation, Multidrug Resistance Protein, Multiple Antibiotic Resistance Regulator Protein, Protein Bldr, Protein Derivative, Unclassified Drug, Archaebacterium, Article, Binding Site, Coding, Dna Binding, Dna Sequence, Gene Targeting, Nonhuman, Priority Journal, Protein Analysis, Protein Function, Structure Analysis, Sulfolobus Solfataricus, Transcription Initiation, X Ray Crystallography, Amino Acid Sequence, Archaeal Proteins, X-Ray, Models, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Trans-Activators, Crenarchaeota,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, Naples, Italy.
Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Naples, Italy
Istituto di Chimica e Biomolecolare-CNR, via Campi Flegrei 34, 80078 Pozzuoli, Italy
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Kusser, A. G., Bertero, M. G., Naji, S., Becker, T., Thomm, M., Beckmann, R., Cramer, P., Structure of an archaeal RNA polymerase (2008) J. Mol. Biol., 376, pp. 303-307
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Wilkinson, S. P., Grove, A., Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins (2006) Curr. Issues Mol. Biol., 8, pp. 51-62
Newberry, K. J., Fuangthong, M., Panmanee, W., Mongkolsuk, S., Brennan, R. G., Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR (2007) Mol. Cell, 28, pp. 652-664
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Wu, R. Y., Zhang, R. G., Zagnitko, O., Dementieva, I., Maltzev, N., Watson, J. D., Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor (2003) J. Biol. Chem., 278, pp. 20240-20244
Ray, S. S., Bonanno, J. B., Chen, H., de Lencastre, H., Wu, S., Tomasz, A., Burley, S. K., X-ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus (2003) Proteins, 50, pp. 170-173
Chin, K. H., Tu, Z. L., Li, J. N., Chou, C. C., Wang, A. H. J., Chou, S. H., The crystal structure of XC1739: a putative multiple antibiotic-resistance repressor (MarR) from Xanthomonas campestris at 1. 8 resolution (2006) Proteins, 65, pp. 239-242
Li, R., Manna, A. C., Dai, S., Cheung, A. L., Zhang, G., Crystal structure of the SarS protein from Staphylococcus aureus (2003) J. Bacteriol., 185, pp. 4219-4225
Laskowski, R. A., MacArthur, M. W., Moss, M. D., Thorton, J. M., PROCHECK: a program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Oh, S. Y., Shin, J. H., Roe, J. H., Dual role of OhrR as a repressor and an activator in response to organic hydroperoxides in Streptomyces coelicolor (2007) J. Bacteriol., 189, pp. 6284-6292
Terwilliger, T. C., Berendzen, J., Automated MAD and MIR structure solution (1999) Acta Crystallogr. Sect. D, 55, pp. 849-861
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. Sect. A, 47, pp. 110-119
Br nger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunsteleve, R. W., Crystallography and NMR system (CNS): a new software system for macromolecular structure determination (1998) Acta Crystallogr. Sect. D, 54, pp. 905-921
Case, D. A., Darden, T. A., Cheatham, T. E., Simmerling III, C. L., Wang, J., Duke, R. E., (2006) AMBER 9, , University of California, San Francisco
Ryckaert, J. -P., Ciccotti, G., Berendsen, H. J. C., Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes (1977) J. Comput. Phys., 23, pp. 327-341
Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteins
Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteins
Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteins
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S * Fusion in Coq(481 views) Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596. Impact Factor:0.415 ViewExport to BibTeXExport to EndNote