3W03

XLF-XRCC4 complex

Summary for 3W03

• Entry DOI: 10.2210/pdb3w03/pdb
• Related: 3Q4F 3RWR 3SR2
• Descriptor: Non-homologous end-joining factor 1, DNA repair protein XRCC4 (2 entities in total)
• Functional Keywords: coiled-coil, nhej, dsbs repair, ku70/80, dna-pkcs, dna ligase iv, dna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9H9Q4 Q13426
• Total number of polymer chains: 4
• Total formula weight: 95392.64

Authors

Wu, Q.,Ochi, T.,Matak-Vinkovic, D.,Robinson, C.V.,Chirgadze, D.Y.,Blundell, T.L. (deposition date: 2012-10-17, release date: 2012-11-07, Last modification date: 2023-11-08)

Primary citation

Wu, Q.,Ochi, T.,Matak-Vinkovic, D.,Robinson, C.V.,Chirgadze, D.Y.,Blundell, T.L.
Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions
Biochem.Soc.Trans., 39:1387-1392, 2011

PubMed Abstract: XRCC4 (X-ray cross-complementation group 4) and XLF (XRCC4-like factor) are two essential interacting proteins in the human NHEJ (non-homologous end-joining) pathway that repairs DNA DSBs (double-strand breaks). The individual crystal structures show that the dimeric proteins are homologues with protomers containing head domains and helical coiled-coil tails related by approximate two-fold symmetry. Biochemical, mutagenesis, biophysical and structural studies have identified the regions of interaction between the two proteins and suggested models for the XLF-XRCC4 complex. An 8.5 Å (1 Å = 0.1 nm) resolution crystal structure of XLF-XRCC4 solved by molecular replacement, together with gel filtration and nano-ESI (nano-electrospray ionization)-MS results, demonstrates that XLF and XRCC4 dimers interact through their head domains and form an alternating left-handed helical structure with polypeptide coiled coils and pseudo-dyads of individual XLF and XRCC4 dimers at right angles to the helical axis.

PubMed: 21936820
DOI: 10.1042/BST0391387

Experimental method

X-RAY DIFFRACTION (8.492 Å)