2fpl: Difference between revisions

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[[Image:2fpl.~~jpg~~|left|200px]]

[[Image:2fpl.png|left|200px]]

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~~'''~~RadA recombinase in complex with AMP-PNP and low concentration of K+~~'''~~

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

~~==Overview==~~

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~~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.

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==About this Structure==

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[[Category: Protein-atp complex]]

[[Category: Rada/adp complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 04~~:10:16 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:35:24 2008''

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-[[Image:2fpl.jpg|left|200px]]
+{{Seed}}
+[[Image:2fpl.png|left|200px]]
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 {{STRUCTURE_2fpl|  PDB=2fpl  |  SCENE=  }}
-'''RadA recombinase in complex with AMP-PNP and low concentration of K+'''
+===RadA recombinase in complex with AMP-PNP and low 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}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Protein-atp complex]]
 [[Category: Rada/adp complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:10:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:35:24 2008''