2FZL

Structure of C-terminal domain of Archaeoglobus fulgidus XPB

Summary for 2FZL

• Entry DOI: 10.2210/pdb2fzl/pdb
• Related: 2FWR
• Descriptor: DNA repair protein RAD25, XPB, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: xpb, nucleotide excision repair, dna repair, dna binding protein
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 1
• Total formula weight: 25730.76

Authors

Fan, L.,Arvai, A.S.,Tainer, J.A. (deposition date: 2006-02-09, release date: 2006-04-18, Last modification date: 2023-08-30)

Primary citation

Fan, L.,Arvai, A.S.,Cooper, P.K.,Iwai, S.,Hanaoka, F.,Tainer, J.A.
Conserved XPB Core Structure and Motifs for DNA Unwinding: Implications for Pathway Selection of Transcription or Excision Repair
Mol.Cell, 22:27-37, 2006

PubMed Abstract: 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.

PubMed: 16600867
DOI: 10.1016/j.molcel.2006.02.017

Experimental method

X-RAY DIFFRACTION (2.9 Å)