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- W1997454893 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." @default.
- W1997454893 created "2016-06-24" @default.
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- W1997454893 date "2007-04-01" @default.
- W1997454893 modified "2023-09-30" @default.
- W1997454893 title "Last Stop on the Road to Repair: Structure of E. coli DNA Ligase Bound to Nicked DNA-Adenylate" @default.
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- W1997454893 doi "https://doi.org/10.1016/j.molcel.2007.02.026" @default.
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