1ir6

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Revision as of 20:17, 24 November 2007

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spinqualitylabelsall models 1ir6, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of exonuclease RecJ bound to manganese

Overview

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 Mn(2+) ion essential for its activity. RecJ has, a novel fold in which two domains are interconnected by a long helix, forming a central groove. Mn(2+) 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.

About this Structure

1IR6 is a Single protein structure of sequence from Thermus thermophilus with MN as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity., Yamagata A, Kakuta Y, Masui R, Fukuyama K, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5908-12. Epub 2002 Apr 23. PMID:11972066

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