2fwr | pdb_00002fwr
Structure of Archaeoglobus Fulgidis XPB
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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 PO4 and IPA 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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