Nucleic Acids Research Advance Access originally published online on February 28, 2007
Nucleic Acids Research 2007 35(6):1787-1801; doi:10.1093/nar/gkl1131
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Nucleic Acids Research, 2007, Vol. 35, No. 6 1787-1801
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
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
1Institute of Biochemical Sciences, National Taiwan University, Taipei 106, 2Institute of Biological Chemistry and 3Institute of Physics, Academia Sinica, Taipei 115, Taiwan
*To whom correspondence should be addressed. Tel: +886-2-27855696; Fax: +886-2-27889759; E-mail: tfwang{at}gate.sinica.edu.tw
Received October 18, 2006. Revised December 4, 2006. Accepted December 12, 2006.
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 ß-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° 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.
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