3bpv: Difference between revisions

Revision as of 12:55, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bpv.png

Template:STRUCTURE 3bpv

Crystal Structure of MarRCrystal Structure of MarR

Template:ABSTRACT PUBMED 18272181

About this StructureAbout this Structure

3BPV is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

Structural insight on the mechanism of regulation of the MarR family of proteins: high-resolution crystal structure of a transcriptional repressor from Methanobacterium thermoautotrophicum., Saridakis V, Shahinas D, Xu X, Christendat D, J Mol Biol. 2008 Mar 28;377(3):655-67. Epub 2008 Jan 11. PMID:18272181

Page seeded by OCA on Sun Jul 27 12:55:06 2008

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-'''Crystal Structure of MarR'''
+===Crystal Structure of MarR===
-==Overview==
+<!--
-Transcriptional regulators belonging to the MarR family are characterized by a winged-helix DNA binding domain. These transcriptional regulators regulate the efflux and influx of phenolic agents in bacteria and archaea. In Escherichia coli, MarR regulates the multiple antibiotic resistance operon and its inactivation produces a multiple antibiotic resistance phenotype. In some organisms, active efflux of drug compounds will produce a drug resistance phenotype, whereas in other organisms, active influx of chlorinated hydrocarbons results in their rapid degradation. Although proteins in the MarR family are regulators of important biological processes, their mechanism of action is not well understood and structural information about how phenolic agents regulate the activity of these proteins is lacking. This article presents the three-dimensional structure of a protein of the MarR family, MTH313, in its apo form and in complex with salicylate, a known inactivator. A comparison of these two structures indicates that the mechanism of regulation involves a large conformational change in the DNA binding lobe. Electrophoretic mobility shift assay and biophysical analyses further suggest that salicylate inactivates MTH313 and prevents it from binding to its promoter region.
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 [[Category: Transcription regulator]]
 [[Category: Winged helix motif]]
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