2fpm: Difference between revisions

Revision as of 04:33, 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:2fpm.png

Template:STRUCTURE 2fpm

RadA recombinase in complex with AMP-PNP and high concentration of K+RadA recombinase in complex with AMP-PNP and high concentration of K+

Template:ABSTRACT PUBMED 16229465

About this StructureAbout this Structure

2FPM is a Single protein structure of sequence from Methanococcus voltae. This structure supersedes the now removed PDB entry 1z4d. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change., Qian X, Wu Y, He Y, Luo Y, Biochemistry. 2005 Oct 25;44(42):13753-61. PMID:16229465

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OCA

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-'''RadA recombinase in complex with AMP-PNP and high concentration of K+'''
+===RadA recombinase in complex with AMP-PNP and high concentration of K+===
-==Overview==
+<!--
-Members of a superfamily of RecA-like recombinases facilitate a central strand exchange reaction in the DNA repair process. Archaeal RadA and Rad51 and eukaryal Rad51 and meiosis-specific DMC1 form a closely related group of recombinases distinct from bacterial RecA. Nevertheless, all such recombinases share a conserved core domain which carries the ATPase site and putative DNA-binding sites. Here we present the crystal structure of an archaeal RadA from Methanococcus voltae (MvRadA) in complex with ADP and Mg2+ at 2.1 A resolution. The crystallized RadA-ADP filament has an extended helical pitch similar to those of previously determined structures in the presence of nonhydrolyzable ATP analogue AMP-PNP. Structural comparison reveals two recurrent conformations with an extensive allosteric effect spanning the ATPase site and the putative DNA-binding L2 region. Varied conformations of the L2 region also imply a dynamic nature of recombinase-bound DNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_16229465}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16229465 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16229465}}
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 [[Category: Protein-atp complex]]
 [[Category: Rada/adp complex]]
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