2fwr

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Revision as of 17:46, 29 January 2008

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spinqualitylabelsall models 2fwr, resolution 2.600Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Archaeoglobus Fulgidis XPB

Overview

The human xeroderma pigmentosum group B (XPB) helicase is essential for, transcription, nucleotide excision repair, and TFIIH functional assembly., Here, we determined crystal structures of an Archaeoglobus fulgidus XPB, homolog (AfXPB) that characterize two RecA-like XPB helicase domains and, discover a DNA damage recognition domain (DRD), a unique RED motif, a, flexible thumb motif (ThM), and implied conformational changes within a, conserved functional core. RED motif mutations dramatically reduce, helicase activity, and the DRD and ThM, which flank the RED motif, appear, structurally as well as functionally analogous to the MutS mismatch, recognition and DNA polymerase thumb domains. Substrate specificity is, altered by DNA damage, such that AfXPB unwinds dsDNA with 3' extensions, but not blunt-ended dsDNA, unless it contains a lesion, as shown for CPD, or (6-4) photoproducts. Together, these results provide an unexpected, mechanism of DNA unwinding with implications for XPB damage verification, in nucleotide excision repair.

About this Structure

2FWR is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.

Reference

Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair., Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, Tainer JA, Mol Cell. 2006 Apr 7;22(1):27-37. PMID:16600867

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