3VNN

Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV

Summary for 3VNN

• Entry DOI: 10.2210/pdb3vnn/pdb
• Related: 1IK9 1X9N 2E2W 3II6 3L2P
• Descriptor: DNA ligase 4 (2 entities in total)
• Functional Keywords: dna ligase, non-homologous end joining, dna repair, xrcc4, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P49917
• Total number of polymer chains: 1
• Total formula weight: 16196.51

Authors

Ochi, T.,Wu, Q.,Chirgadze, D.Y.,Grossmann, J.G.,Bolanos-Garcia, V.M.,Blundell, T.L. (deposition date: 2012-01-17, release date: 2012-06-20, Last modification date: 2024-03-20)

Primary citation

Ochi, T.,Wu, Q.,Chirgadze, D.Y.,Grossmann, J.G.,Bolanos-Garcia, V.M.,Blundell, T.L.
Structural insights into the role of domain flexibility in human DNA ligase IV
Structure, 20:1212-1222, 2012

PubMed Abstract: Knowledge of the architecture of DNA ligase IV (LigIV) and interactions with XRCC4 and XLF-Cernunnos is necessary for understanding its role in the ligation of double-strand breaks during nonhomologous end joining. Here we report the structure of a subdomain of the nucleotidyltrasferase domain of human LigIV and provide insights into the residues associated with LIG4 syndrome. We use this structural information together with the known structures of the BRCT/XRCC4 complex and those of LigIV orthologs to interpret small-angle X-ray scattering of LigIV in complex with XRCC4 and size exclusion chromatography of LigIV, XRCC4, and XLF-Cernunnos. Our results suggest that the flexibility of the catalytic region is limited in a manner that affects the formation of the LigIV/XRCC4/XLF-Cernunnos complex.

PubMed: 22658747
DOI: 10.1016/j.str.2012.04.012

Experimental method

X-RAY DIFFRACTION (2.903 Å)