4QBL

VRR_NUC domain protein

4QBL の概要

• エントリーDOI: 10.2210/pdb4qbl/pdb
• 関連するPDBエントリー: 4QBN 4QBO
• 分子名称: VRR-NUC, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: nuclease, hydrolase
• 由来する生物種: Psychrobacter sp.
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 97851.67

構造登録者

Smerdon, S.J.,Pennell, S.,Li, J. (登録日: 2014-05-08, 公開日: 2014-09-10, 最終更新日: 2024-11-06)

主引用文献

Pennell, S.,Declais, A.C.,Li, J.,Haire, L.F.,Berg, W.,Saldanha, J.W.,Taylor, I.A.,Rouse, J.,Lilley, D.M.,Smerdon, S.J.
FAN1 activity on asymmetric repair intermediates is mediated by an atypical monomeric virus-type replication-repair nuclease domain.
Cell Rep, 8:84-93, 2014

PubMed Abstract: FAN1 is a structure-selective DNA repair nuclease with 5' flap endonuclease activity, involved in the repair of interstrand DNA crosslinks. It is the only eukaryotic protein with a virus-type replication-repair nuclease ("VRR-Nuc") "module" that commonly occurs as a standalone domain in many bacteria and viruses. Crystal structures of three representatives show that they structurally resemble Holliday junction resolvases (HJRs), are dimeric in solution, and are able to cleave symmetric four-way junctions. In contrast, FAN1 orthologs are monomeric and cleave 5' flap structures in vitro, but not Holliday junctions. Modeling of the VRR-Nuc domain of FAN1 reveals that it has an insertion, which packs against the dimerization interface observed in the structures of the viral/bacterial VRR-Nuc proteins. We propose that these additional structural elements in FAN1 prevent dimerization and bias specificity toward flap structures.

PubMed: 24981866
DOI: 10.1016/j.celrep.2014.06.001

実験手法

X-RAY DIFFRACTION (2 Å)