3W1B

Crystal Structure of Human DNA ligase IV-Artemis Complex (Mercury Derivative)

Summary for 3W1B

• Entry DOI: 10.2210/pdb3w1b/pdb
• Related: 1IK9 1X9N 2E2W 3II6 3L2P 3VNN 3W1G 3W5O
• Descriptor: DNA ligase 4, Artemis-derived peptide, ADENOSINE MONOPHOSPHATE, ... (6 entities in total)
• Functional Keywords: dna ligase, non-homologous end joining, dna repair, xrcc4, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P49917 Q96SD1
• Total number of polymer chains: 2
• Total formula weight: 74104.13

Authors

Ochi, T.,Blundell, T.L. (deposition date: 2012-11-14, release date: 2013-04-03, Last modification date: 2024-10-16)

Primary citation

Ochi, T.,Gu, X.,Blundell, T.L.
Structure of the catalytic region of DNA ligase IV in complex with an artemis fragment sheds light on double-strand break repair
Structure, 21:672-679, 2013

PubMed 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.

PubMed: 23523427
DOI: 10.1016/j.str.2013.02.014

Experimental method

X-RAY DIFFRACTION (2.4 Å)