2fbv

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(New page: 200px<br /> <applet load="2fbv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fbv, resolution 2.40&Aring;" /> '''WRN exonuclease, Mn...)
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Revision as of 19:56, 12 November 2007

Image:2fbv.gif

2fbv, resolution 2.40Å

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WRN exonuclease, Mn complex

Contents

Overview

WRN is unique among the five human RecQ DNA helicases in having a, functional exonuclease domain (WRN-exo) and being defective in the, premature aging and cancer-related disorder Werner syndrome. Here, we, characterize WRN-exo crystal structures, biochemical activity and, participation in DNA end joining. Metal-ion complex structures, active, site mutations and activity assays reveal a nuclease mechanism mediated by, two metal ions. The DNA end-binding Ku70/80 complex specifically, stimulates WRN-exo activity, and structure-based mutational inactivation, of WRN-exo alters DNA end joining in human cells. We furthermore establish, structural and biochemical similarities of WRN-exo to DnaQ-family, replicative proofreading exonucleases, describing WRN-specific adaptations, consistent with double-stranded DNA specificity and functionally important, conformational changes. These results indicate WRN-exo is a human DnaQ, family member and support DnaQ-like proofreading activities stimulated by, Ku70/80, with implications for WRN functions in age-related pathologies, and maintenance of genomic integrity.

Disease

Known diseases associated with this structure: Werner syndrome OMIM:[604611]

About this Structure

2FBV is a Single protein structure of sequence from Homo sapiens with MN as ligand. Full crystallographic information is available from OCA.

Reference

WRN exonuclease structure and molecular mechanism imply an editing role in DNA end processing., Perry JJ, Yannone SM, Holden LG, Hitomi C, Asaithamby A, Han S, Cooper PK, Chen DJ, Tainer JA, Nat Struct Mol Biol. 2006 May;13(5):414-22. Epub 2006 Apr 23. PMID:16622405

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