The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity

Atsushi Yamagata, Yoshimitsu Kakuta, Ryoji Masui, Keiichi Fukuyama

Research output: Contribution to journalArticlepeer-review

73 Citations (Scopus)

Abstract

RecJ, a 5′ to 3′ exonuclease specific for single-stranded DNA, functions in DNA repair and recombination systems. We determined the crystal structure of RecJ bound to Mn2+ ion essential for its activity. RecJ has a novel fold in which two domains are interconnected by a long helix, forming a central groove. Mn2+ is located on the wall of the groove and is coordinated by conserved residues characteristic of a family of phosphoesterases that includes RecJ proteins. The groove is composed of residues conserved among RecJ proteins and is positively charged. These findings and the narrow width of the groove indicate that the groove binds single- instead of double-stranded DNA.

Original languageEnglish
Pages (from-to)5908-5912
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number9
DOIs
Publication statusPublished - Apr 30 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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