1t4g

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Revision as of 00:51, 21 November 2007

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spinqualitylabelsall models 1t4g, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ATPase in complex with AMP-PNP

Overview

Homologous recombination of DNA plays crucial roles in repairing severe, DNA damage and in generating genetic diversity. The process is facilitated, by a superfamily of recombinases: bacterial RecA, archaeal RadA and Rad51, and eukaryal Rad51 and DMC1. These recombinases share a common, ATP-dependent filamentous quaternary structure for binding DNA and, facilitating strand exchange. We have determined the crystal structure of, Methanococcus voltae RadA in complex with the ATP analog AMP-PNP at 2.0 A, resolution. The RadA filament is a 106.7 A pitch helix with six subunits, per turn. The DNA binding loops L1 and L2 are located in close proximity, to the filament axis. The ATP analog is buried between two RadA subunits, a feature similar to that of the active filament of Escherichia coli RecA, revealed by electron microscopy. The disposition of the N-terminal domain, suggests a role of the Helix-hairpin-Helix motif in binding, double-stranded DNA.

About this Structure

1T4G is a Single protein structure of sequence from Methanococcus voltae with MG and ANP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation., Wu Y, He Y, Moya IA, Qian X, Luo Y, Mol Cell. 2004 Aug 13;15(3):423-35. PMID:15304222

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