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PMID:23523427

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Citation

Ochi, T, Gu, X and Blundell, TL (2013) Structure of the catalytic region of DNA ligase IV in complex with an Artemis fragment sheds light on double-strand break repair. Structure 21:672-9

Abstract

Nonhomologous end joining (NHEJ) is central to the repair of double-stranded DNA breaks throughout the cell cycle and plays roles in the development of the immune system. Although three-dimensional structures of most components of NHEJ have been defined, those of the catalytic region of DNA ligase IV (LigIV), a specialized DNA ligase known to work in NHEJ, and of Artemis have remained unresolved. Here, we report the crystal structure at 2.4 Å resolution of the catalytic region of LigIV (residues 1-609) in complex with an Artemis peptide. We describe interactions of the DNA-binding domain of LigIV with the continuous epitope of Artemis, which, together, form a three-helix bundle. A kink in the first helix of LigIV introduced by a conserved VPF motif gives rise to a hydrophobic pocket, which accommodates a conserved tryptophan from Artemis. We provide structural insights into features of LigIV among human DNA ligases.

Links

PubMed PMC3664939 Online version:10.1016/j.str.2013.02.014

Keywords

Catalysis; Crystallography; DNA Breaks, Double-Stranded; DNA End-Joining Repair/genetics; DNA Ligases/chemistry; DNA Ligases/isolation & purification; Electrophoresis, Polyacrylamide Gel; Humans; Models, Molecular; Multiprotein Complexes/chemistry; Multiprotein Complexes/metabolism; Nuclear Proteins/chemistry; Nuclear Proteins/metabolism; Protein Conformation

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:DNLI4

GO:0003909: DNA ligase activity

ECO:0000314:

F

The SDS-PAGE gel of fractions eluted from a heparin column and from a Superdex column led to protein bands forming next to the same molecular weight markers.

complete
CACAO 9406

See also

References

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