Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.

Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.

An elegantly simple and probably ancient molecular mechanism of allostery is described for the Escherichia coli arginine repressor ArgR, the master feedback regulator of transcription in L-arginine metabolism. Molecular dynamics simulations with ArgRC, the hexameric domain that binds L-arginine with...

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Bibliographic Details
Main Authors: Rebecca Strawn, Milan Melichercik, Michael Green, Thomas Stockner, Jannette Carey, Rüdiger Ettrich
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2010-06-01
Series:PLoS Computational Biology
Online Access:http://europepmc.org/articles/PMC2880562?pdf=render

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http://europepmc.org/articles/PMC2880562?pdf=render

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