1IR6
Crystal structure of exonuclease RecJ bound to manganese
Summary for 1IR6
| Entry DOI | 10.2210/pdb1ir6/pdb |
| Descriptor | exonuclease RecJ, MANGANESE (II) ION (2 entities in total) |
| Functional Keywords | manganese, dna repair, dna recombination, nuclease, single-stranded dna, two domains interconnected by alpha-helix, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 45951.91 |
| Authors | Yamagata, A.,Kakuta, Y.,Masui, R.,Fukuyama, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-09-11, release date: 2002-05-15, Last modification date: 2023-12-27) |
| Primary citation | Yamagata, A.,Kakuta, Y.,Masui, R.,Fukuyama, K. The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity. Proc.Natl.Acad.Sci.USA, 99:5908-5912, 2002 Cited by PubMed 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 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. PubMed: 11972066DOI: 10.1073/pnas.092547099 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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