2bhn
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(New page: 200px<br /><applet load="2bhn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bhn, resolution 3.20Å" /> '''XPF FROM AEROPYRUM P...)
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Revision as of 16:24, 29 January 2008
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XPF FROM AEROPYRUM PERNIX
Overview
The XPF/Mus81 structure-specific endonucleases cleave double-stranded DNA, (dsDNA) within asymmetric branched DNA substrates and play an essential, role in nucleotide excision repair, recombination and genome integrity. We, report the structure of an archaeal XPF homodimer alone and bound to, dsDNA. Superposition of these structures reveals a large domain movement, upon binding DNA, indicating how the (HhH)(2) domain and the nuclease, domain are coupled to allow the recognition of, double-stranded/single-stranded DNA junctions. We identify two, nonequivalent DNA-binding sites and propose a model in which XPF distorts, the 3' flap substrate in order to engage both binding sites and promote, strand cleavage. The model rationalises published biochemical data and, implies a novel role for the ERCC1 subunit of eukaryotic XPF complexes.
About this Structure
2BHN is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.
Reference
Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition., Newman M, Murray-Rust J, Lally J, Rudolf J, Fadden A, Knowles PP, White MF, McDonald NQ, EMBO J. 2005 Mar 9;24(5):895-905. Epub 2005 Feb 17. PMID:15719018
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