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

Result code in 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>

Alternative codes found

RIV/67179843:_____/14:00435268

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2014

Confidentiality

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

Name of the periodical

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Volume of the periodical

20

Issue of the periodical within the volume

7

Country of publishing house

US - UNITED STATES

Number of pages

9

Pages from-to

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UT code for WoS article

000339884800019

EID of the result in the Scopus database

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