2fpk: Difference between revisions
New page: left|200px<br /><applet load="2fpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fpk, resolution 2.10Å" /> '''RadA recombinase in ... |
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[[Image:2fpk.jpg|left|200px]]<br /><applet load="2fpk" size=" | [[Image:2fpk.jpg|left|200px]]<br /><applet load="2fpk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fpk, resolution 2.10Å" /> | caption="2fpk, resolution 2.10Å" /> | ||
'''RadA recombinase in complex with ADP'''<br /> | '''RadA recombinase in complex with ADP'''<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== | ||
2FPK 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 ADP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | 2FPK 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=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1Z4B. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPK 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 17:23:48 2008'' | ||
Revision as of 18:23, 21 February 2008
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RadA recombinase in complex with ADP
OverviewOverview
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 StructureAbout this Structure
2FPK is a Single protein structure of sequence from Methanococcus voltae with , and as ligands. This structure supersedes the now removed PDB entry 1Z4B. 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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