1ir6

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Thermus thermophilus | Fukuyama, K. | Kakuta, Y. | Masui, R. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yamagata, A. | Dna recombination | Dna repair | Manganese | Nuclease | Riken structural genomics/proteomics initiative | Rsgi | Single-stranded dna | Structural genomic | Two domains interconnected by alpha-helix