1FU1

CRYSTAL STRUCTURE OF HUMAN XRCC4

Summary for 1FU1

• Entry DOI: 10.2210/pdb1fu1/pdb
• Descriptor: DNA REPAIR PROTEIN XRCC4, ACETIC ACID (3 entities in total)
• Functional Keywords: helix-turn-helix, helix bundle, gene regulation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 47805.07

Authors

Junop, M.,Modesti, M.,Guarne, A.,Gellert, M.,Yang, W. (deposition date: 2000-09-13, release date: 2000-12-11, Last modification date: 2024-11-06)

Primary citation

Junop, M.S.,Modesti, M.,Guarne, A.,Ghirlando, R.,Gellert, M.,Yang, W.
Crystal structure of the Xrcc4 DNA repair protein and implications for end joining.
EMBO J., 19:5962-5970, 2000

PubMed Abstract: XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ) in all eukaryotes and, in particular, V(D)J recombination in vertebrates. Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends in the last step of V(D)J recombination and NHEJ to repair double strand breaks. XRCC4-defective cells are extremely sensitive to ionizing radiation, and disruption of the XRCC4 gene results in embryonic lethality in mice. Here we report the crystal structure of a functional fragment of Xrcc4 at 2.7 A resolution. Xrcc4 protein forms a strikingly elongated dumb-bell-like tetramer. Each of the N-terminal globular head domains consists of a beta-sandwich and a potentially DNA-binding helix- turn-helix motif. The C-terminal stalk comprising a single alpha-helix >120 A in length is partly incorporated into a four-helix bundle in the Xrcc4 tetramer and partly involved in interacting with ligase IV. The Xrcc4 structure suggests a possible mode of coupling ligase IV association with DNA binding for effective ligation of DNA ends.

PubMed: 11080143
DOI: 10.1093/emboj/19.22.5962

Experimental method

X-RAY DIFFRACTION (2.7 Å)