2dfl

From Proteopedia

Revision as of 12:05, 23 January 2008

Crystal structure of left-handed RadA filament

Overview

The RecA family of proteins mediates homologous recombination, an, evolutionarily conserved pathway that maintains genomic stability by, protecting against DNA double strand breaks. RecA proteins are thought to, facilitate DNA strand exchange reactions as closed-rings or as, right-handed helical filaments. Here, we report the crystal structure of a, left-handed Sulfolobus solfataricus RadA helical filament. Each protomer, in this left-handed filament is linked to its neighbour via interactions, of a beta-strand polymerization motif with the neighbouring ATPase domain., Immediately following the polymerization motif, we identified an, evolutionarily conserved hinge region (a subunit rotation motif) in which, a 360 degrees clockwise axial rotation accompanies stepwise structural, transitions from a closed ring to the AMP-PNP right-handed filament, then, to an overwound right-handed filament and finally to the left-handed, filament. Additional structural and functional analyses of wild-type and, mutant proteins confirmed that the subunit rotation motif is crucial for, enzymatic functions of RecA family proteins. These observations support, the hypothesis that RecA family protein filaments may function as rotary, motors.

About this Structure

2DFL is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins., Chen LT, Ko TP, Chang YC, Lin KA, Chang CS, Wang AH, Wang TF, Nucleic Acids Res. 2007;35(6):1787-801. Epub 2007 Feb 28. PMID:17329376

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