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2owo
From Proteopedia
| |||||||
| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | ligA (Escherichia coli) | ||||||
| Activity: | DNA ligase (NAD(+)), with EC number 6.5.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Last Stop on the Road to Repair: Structure of E.coli DNA Ligase Bound to Nicked DNA-Adenylate
Overview
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.
About this Structure
2OWO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate., Nandakumar J, Nair PA, Shuman S, Mol Cell. 2007 Apr 27;26(2):257-71. PMID:17466627
Page seeded by OCA on Thu Mar 20 18:05:30 2008
Categories: DNA ligase (NAD(+)) | Escherichia coli | Single protein | Nair, P A. | Nandakumar, J. | Shuman, S. | AMP | SO4 | ZN | Dna | Ligase | Protein/dna complex
