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Mol Cell. 2007 Apr 27;26(2):257-71.

Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate.

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1
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.

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.

PMID:
17466627
DOI:
10.1016/j.molcel.2007.02.026
[Indexed for MEDLINE]
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