2oqr: Difference between revisions

Revision as of 05:09, 28 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:2oqr.png

Template:STRUCTURE 2oqr

The structure of the response regulator RegX3 from Mycobacterium tuberculosisThe structure of the response regulator RegX3 from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 17942407

About this StructureAbout this Structure

2OQR is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state., King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA, J Biol Chem. 2007 Dec 28;282(52):37717-29. Epub 2007 Oct 16. PMID:17942407

Page seeded by OCA on Mon Jul 28 05:09:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The structure of the response regulator RegX3 from Mycobacterium tuberculosis'''
+===The structure of the response regulator RegX3 from Mycobacterium tuberculosis===
-==Overview==
+<!--
-The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 A(2) per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.
+The line below this paragraph, {{ABSTRACT_PUBMED_17942407}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17942407 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17942407}}
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