4QBL

VRR_NUC domain protein

Summary for 4QBL

• Entry DOI: 10.2210/pdb4qbl/pdb
• Related: 4QBN 4QBO
• Descriptor: VRR-NUC, MAGNESIUM ION (3 entities in total)
• Functional Keywords: nuclease, hydrolase
• Biological source: Psychrobacter sp.
• Total number of polymer chains: 6
• Total formula weight: 97851.67

Authors

Smerdon, S.J.,Pennell, S.,Li, J. (deposition date: 2014-05-08, release date: 2014-09-10, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)