2gdj: Difference between revisions
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'''Delta-62 RADA recombinase in complex with AMP-PNP and magnesium''' | '''Delta-62 RADA recombinase in complex with AMP-PNP and magnesium''' | ||
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[[Category: Qian, X.]] | [[Category: Qian, X.]] | ||
[[Category: Wu, Y.]] | [[Category: Wu, Y.]] | ||
[[Category: | [[Category: Atpase]] | ||
[[Category: | [[Category: Protein-atp complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:58:53 2008'' | |||
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Revision as of 04:58, 4 May 2008
Delta-62 RADA recombinase in complex with AMP-PNP and magnesium
OverviewOverview
Proteins in the RecA/RadA/Rad51 family form helical filaments on DNA that function in homologous recombination. While these proteins all have the same highly conserved ATP binding core, the RadA/Rad51 proteins have an N-terminal domain that shows no homology with the C-terminal domain found in RecA. Both the Rad51 N-terminal and RecA C-terminal domains have been shown to bind DNA, but no role for these domains has been established. We show that RadA filaments can be trapped in either an inactive or active conformation with respect to the ATPase and that activation involves a large rotation of the subunit aided by the N-terminal domain. The G103E mutation within the yeast Rad51 N-terminal domain inactivates the filament by failing to make proper contacts between the N-terminal domain and the core. These results show that the N-terminal domains play a regulatory role in filament activation and highlight the modular architecture of the recombination proteins.
About this StructureAbout this Structure
2GDJ is a Single protein structure of sequence from Methanococcus voltae. Full crystallographic information is available from OCA.
ReferenceReference
The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity., Galkin VE, Wu Y, Zhang XP, Qian X, He Y, Yu X, Heyer WD, Luo Y, Egelman EH, Structure. 2006 Jun;14(6):983-92. PMID:16765891 Page seeded by OCA on Sun May 4 04:58:53 2008