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Article

Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D.

Proceedings of the National Academy of Sciences of the United States of America - 7 Feb 2006

Zhu Hui, Nandakumar Jayakrishnan, Aniukwu Jideofor, Wang Li Kai, Glickman Michael S, Lima Christopher D, Shuman Stewart

Abstract excerpt

DNA ligase D (LigD) is a large polyfunctional protein that participates in a recently discovered pathway of nonhomologous end-joining in bacteria. LigD consists of an ATP-dependent ligase domain fused to a polymerase domain (Pol) and a phosphoesterase module. The Pol activity is remarkable for its dependence on manganese, its ability to perform templated and nontemplated primer extension reactions, and its...

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Identifiers

PMID: 16446439
DOI: 10.1073/pnas.0509083103
PMCID: PMC1413644

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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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