Binding-competent states for L-arginine in E. coli arginine repressor apoprotein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887438" target="_blank" >RIV/60076658:12310/14:43887438 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/14:00435268

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs00894-014-2330-5" target="_blank" >http://link.springer.com/article/10.1007%2Fs00894-014-2330-5</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-014-2330-5" target="_blank" >10.1007/s00894-014-2330-5</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Binding-competent states for L-arginine in E. coli arginine repressor apoprotein

Popis výsledku v původním jazyce

Arginine repressor of E. coli is a multifunctional hexameric protein that provides feedback regulation of arginine metabolism upon activation by the negatively cooperative binding of L-arginine. Interpretation of this complex system requires an understanding of the protein's conformational landscape. The similar to 50 kDa hexameric C-terminal domain was studied by 100 ns molecular dynamics simulations in the presence and absence of the six L-arg ligands that bind at the trimer-trimer interface. A rotational shift between trimers followed by rotational oscillation occurs in the production phase of the simulations only when L-arg is absent. Analysis of the system reveals that the degree of rotation is correlated with the number of hydrogen bonds across the trimer interface. The trajectory presents frames with one or more apparently open binding sites into which one L-arg could be docked successfully in three different instances, indicating that a binding-competent state of the system is

Název v anglickém jazyce

Binding-competent states for L-arginine in E. coli arginine repressor apoprotein

Popis výsledku anglicky

Arginine repressor of E. coli is a multifunctional hexameric protein that provides feedback regulation of arginine metabolism upon activation by the negatively cooperative binding of L-arginine. Interpretation of this complex system requires an understanding of the protein's conformational landscape. The similar to 50 kDa hexameric C-terminal domain was studied by 100 ns molecular dynamics simulations in the presence and absence of the six L-arg ligands that bind at the trimer-trimer interface. A rotational shift between trimers followed by rotational oscillation occurs in the production phase of the simulations only when L-arg is absent. Analysis of the system reveals that the degree of rotation is correlated with the number of hydrogen bonds across the trimer interface. The trajectory presents frames with one or more apparently open binding sites into which one L-arg could be docked successfully in three different instances, indicating that a binding-competent state of the system is

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Svazek periodika

20

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

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Kód UT WoS článku

000339884800019

EID výsledku v databázi Scopus

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