2FZ4

Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB

2FZ4 の概要

• エントリーDOI: 10.2210/pdb2fz4/pdb
• 分子名称: DNA repair protein RAD25 (2 entities in total)
• 機能のキーワード: reca-like domain, dna damage recognition domain, dna binding protein
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26826.39

構造登録者

Fan, L.,Tainer, J.A. (登録日: 2006-02-09, 公開日: 2006-04-18, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)