A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima(437 views) Ruggiero A, Dattelbaum JD, Staiano M, Berisio R, D'Auria S, Vitagliano L
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2014 May 15; 9(5): e96560-e96560.
Keywords: Arginine, Binding Protein, Protein Tmargbp, Unclassified Drug, Abc Transporter, Bacterial Protein, Carrier Protein, Ligand, Protein Binding, Amino Acid Sequence, Analytic Method, Article, Binding Site, Carboxy Terminal Sequence, Computer Model, Controlled Study, Dimerization, Molecular Dynamics, Multiwavelength Anomalous Diffraction, Nonhuman, Polyacrylamide Gel Electrophoresis, Protein Conformation, Protein Domain, Protein Interaction, Protein Structure, Simulation, Single Wavelength Anomalous Dispersion, Structure Analysis, Thermotoga Maritima, Calorimetry, Chemistry, Mass Spectrometry, Molecular Genetics, Protein Multimerization, Protein Quaternary Structure, Protein Tertiary Structure, Sequence Homology, Temperature, X Ray Crystallography, Atp-Binding Cassette Transporters, X-Ray, Molecular Sequence Data, Atp-Binding Cassette Transporters Chemistry, Arginine Chemistry, Bacterial Proteins Chemistry, Carrier Proteins Chemistry, Thermotoga Maritima Chemistry,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Napoli, Italy
Department of Chemistry, University of Richmond, Richmond, VA, United States
Laboratory for Molecular Sensing, IBP, CNR, Naples, Italy
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Berntsson, R. P., Smits, S. H., Schmitt, L., Slotboom, D. J., Poolman, B., A structural classification of substrate-binding proteins (2010) Febs Letters, 584, pp. 2606-2617
Lee, R. A., Razaz, M., Hayward, S., The DynDom database of protein domain motions (2003) Bioinformatics, 19 (10), pp. 1290-1291. , DOI 10. 1093/bioinformatics/btg137
Liu, Y., Hart, P. J., Schlunegger, M. P., Eisenberg, D., The crystal structure of a 3D domain-swapped dimer of RNase A at a 2. 1-A resolution (1998) Proceedings of the National Academy of Sciences of the United States of America, 95, pp. 3437-3442
Cuneo, M. J., Changela, A., Miklos, A. E., Beese, L. S., Krueger, J. K., Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport (2008) The Journal of Biological Chemistry, 283, pp. 32812-32820
Stamp, A. L., Owen, P., El Omari, K., Lockyer, M., Lamb, H. K., Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351 (2011) Proteins-Structure Function and Bioinformatics, 79, pp. 2352-2357
Makhatadze, G. I., Loladze, V. V., Gribenko, A. V., Lopez, M. M., Mechanism of Thermostabilization in a Designed Cold Shock Protein with Optimized Surface Electrostatic Interactions (2004) Journal of Molecular Biology, 336 (4), pp. 929-942. , DOI 10. 1016/j. jmb. 2003. 12. 058
Winn, M. D., Murshudov, G. N., Papiz, M. Z., Macromolecular TLS Refinement in REFMAC at Moderate Resolutions (2003) Methods in Enzymology, 374, pp. 300-321. , DOI 10. 1016/S0076-6879 (03) 74014-2
Karplus, P. A., Experimentally observed conformation-dependent geometry and hidden strain in proteins (1996) Protein Science: A Publication of the Protein Society, 5, pp. 1406-1420
A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima
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