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"Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate." |
Nandakumar J, Nair PA, Shuman S |
Published April 27, 2007 in Mol Cell volume 26 .
Pubmed ID: 17466627
Abstract:
| NAD(+)-dependent DNA ligases (LigA) are ubiquitous in bacteria and essential for growth. Their distinctive substrate specificity and domain organization vis-a-vis human ATP-dependent ligases make them outstanding targets for anti-infective drug discovery. We report here the 2.3 A crystal structure of Escherichia coli LigA bound to an adenylylated nick, which captures LigA in a state poised for strand closure and reveals the basis for nick recognition. LigA envelopes the DNA within a protein clamp. Large protein domain movements and remodeling of the active site orchestrate progression through the three chemical steps of the ligation reaction. The structure inspires a strategy for inhibitor design. |
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Last modification of this entry: Oct. 6, 2010
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