2fpm
From Proteopedia
(New page: 200px<br /><applet load="2fpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fpm, resolution 2.00Å" /> '''RadA recombinase in ...) |
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| - | [[Image:2fpm.jpg|left|200px]]<br /><applet load="2fpm" size=" | + | [[Image:2fpm.jpg|left|200px]]<br /><applet load="2fpm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fpm, resolution 2.00Å" /> | caption="2fpm, resolution 2.00Å" /> | ||
'''RadA recombinase in complex with AMP-PNP and high concentration of K+'''<br /> | '''RadA recombinase in complex with AMP-PNP and high concentration of K+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Members of a superfamily of RecA-like recombinases facilitate a central | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2FPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae] with MG, K and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2FPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1Z4D. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: He, Y.]] | [[Category: He, Y.]] | ||
[[Category: Luo, Y.]] | [[Category: Luo, Y.]] | ||
| - | [[Category: Moya, I | + | [[Category: Moya, I A.]] |
[[Category: Qian, X.]] | [[Category: Qian, X.]] | ||
[[Category: Wu, Y.]] | [[Category: Wu, Y.]] | ||
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[[Category: rada/adp complex]] | [[Category: rada/adp complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:50 2008'' |
Revision as of 15:23, 21 February 2008
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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.
About this Structure
2FPM is a Single protein structure of sequence from Methanococcus voltae with , and as ligands. This structure supersedes the now removed PDB entry 1Z4D. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:23:50 2008
Categories: Methanococcus voltae | Single protein | He, Y. | Luo, Y. | Moya, I A. | Qian, X. | Wu, Y. | ANP | K | MG | Atpase | Co-factors | Potassium-dependence | Protein-atp complex | Rada/adp complex
