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Article

Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D.

The Journal of biological chemistry - 12 May 2006

Akey David, Martins Alexandra, Aniukwu Jideofor, Glickman Michael S, Shuman Stewart, Berger James M

Abstract excerpt

DNA ligase D (LigD) is a large polyfunctional enzyme involved in nonhomologous end-joining (NHEJ) in mycobacteria. LigD consists of a C-terminal ATP-dependent ligase domain fused to upstream polymerase and phosphoesterase modules. Here we report the 2.4 angstroms crystal structure of the ligase domain of Mycobacterium LigD, captured as the covalent ligase-AMP intermediate with a divalent metal in the active site....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16476729
DOI: 10.1074/jbc.M513550200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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