Počet záznamů: 1
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 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues Tvůrce(i) Strawn, R. (US)
Melicherčík, Milan (UEK-B)
Green, M. (US)
Stockner, T. (AT)
Carey, J. (US)
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAICelkový počet autorů 6 Zdroj.dok. PLoS Computational Biology - ISSN 1553-734X
Roč. 6, č. 6 (2010), s. 1-12Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova molecular-dynamics simulations ; free-energy calculations ; structural basis ; DNA-binding domain ; bacillus-stearothermophilus ; T4 lysozyme ; proteins ; hemoglobin ; model ; affinity Vědní obor RIV EH - Ekologie - společenstva CEP LC06010 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GAP207/10/1934 GA ČR - Grantová agentura ČR CEZ AV0Z60870520 - UEK-B (2005-2011) UT WOS 000279341000007 DOI 10.1371/journal.pcbi.1000801 Anotace 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. Pracoviště Ústav výzkumu globální změny Kontakt Nikola Šviková, svikova.n@czechglobe.cz, Tel.: 511 192 268 Rok sběru 2012
Počet záznamů: 1