2OWO

Last Stop on the Road to Repair: Structure of E.coli DNA Ligase Bound to Nicked DNA-Adenylate

Summary for 2OWO

• Entry DOI: 10.2210/pdb2owo/pdb
• Descriptor: 26-MER, 5'-D(*AP*CP*AP*AP*TP*TP*GP*CP*GP*AP*CP*(OMC)P*C)-3', 5'-D(*CP*AP*CP*TP*AP*TP*CP*GP*GP*AP*AP*TP*G)-3', ... (8 entities in total)
• Functional Keywords: dna, ligase, protein-dna complex, ligase-dna complex, ligase/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 90457.24

Authors

Shuman, S.,Nandakumar, J.,Nair, P.A. (deposition date: 2007-02-16, release date: 2007-05-15, Last modification date: 2023-08-30)

Primary citation

Nandakumar, J.,Nair, P.A.,Shuman, S.
Last Stop on the Road to Repair: Structure of E. coli DNA Ligase Bound to Nicked DNA-Adenylate.
Mol.Cell, 26:257-271, 2007

PubMed 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.

PubMed: 17466627
DOI: 10.1016/j.molcel.2007.02.026

Experimental method

X-RAY DIFFRACTION (2.3 Å)