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Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues
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SYSNO ASEP 0359496 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues Author(s) Strawn, R. (US)
Melicherčík, Milan (UEK-B)
Green, M. (US)
Stockner, T. (AT)
Carey, J. (US)
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAINumber of authors 6 Source Title PLoS Computational Biology - ISSN 1553-734X
Roč. 6, č. 6 (2010), s. 1-12Number of pages 12 s. Language eng - English Country US - United States Keywords molecular-dynamics simulations ; free-energy calculations ; structural basis ; DNA-binding domain ; bacillus-stearothermophilus ; T4 lysozyme ; proteins ; hemoglobin ; model ; affinity Subject RIV EH - Ecology, Behaviour R&D Projects LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GAP207/10/1934 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z60870520 - UEK-B (2005-2011) UT WOS 000279341000007 DOI 10.1371/journal.pcbi.1000801 Annotation A controversial prediction of the famous allostery model of Monod, Wyman, and Changeux is that constraints imposed on protein subunits by multimerization are relaxed by ligand binding, but with conservation of symmetry in partially-liganded states. Interpretation of thermodynamic ligand-binding data through the lens of molecular dynamics simulation has led to structural and energetic description of such a state for the hexameric Escherichia coli arginine repressor, which displays strong negative cooperativity of L-arginine binding. The results indicate that partially-liganded states can be structurally symmetric despite their conceptual asymmetry. The symmetric relaxed state is visualized as a multimer with all subunits anchored near the center, and with motions transferred to the periphery of the assembly. Thus, even during sequential filling of binding sites, symmetry can be maintained by exploiting the dynamics of the assembly and the distributed nature of its cohesive free energy. Workplace Global Change Research Institute Contact Nikola Šviková, svikova.n@czechglobe.cz, Tel.: 511 192 268 Year of Publishing 2012
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