7BGF

CRYSTAL STRUCTURE OF THE N-TERMINAL DIMERIC COILED COIL OF THE HUMAN CTIP PROTEIN

Summary for 7BGF

• Entry DOI: 10.2210/pdb7bgf/pdb
• Descriptor: DNA endonuclease RBBP8,CtIP/RBBP8 (2 entities in total)
• Functional Keywords: coiled coil, dimer, dna repair, homologous recombination, dna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 30546.55

Authors

Morton, C.R.,Pellegrini, L. (deposition date: 2021-01-07, release date: 2021-06-30, Last modification date: 2024-05-01)

Primary citation

Morton, C.R.,Rzechorzek, N.J.,Maman, J.D.,Kuramochi, M.,Sekiguchi, H.,Rambo, R.,Sasaki, Y.C.,Davies, O.R.,Pellegrini, L.
Structural basis for the coiled-coil architecture of human CtIP.
Open Biology, 11:210060-210060, 2021

PubMed Abstract: The DNA repair factor CtIP has a critical function in double-strand break (DSB) repair by homologous recombination, promoting the assembly of the repair apparatus at DNA ends and participating in DNA-end resection. However, the molecular mechanisms of CtIP function in DSB repair remain unclear. Here, we present an atomic model for the three-dimensional architecture of human CtIP, derived from a multi-disciplinary approach that includes X-ray crystallography, small-angle X-ray scattering (SAXS) and diffracted X-ray tracking (DXT). Our data show that CtIP adopts an extended dimer-of-dimers structure, in agreement with a role in bridging distant sites on chromosomal DNA during the recombinational repair. The zinc-binding motif in the CtIP N-terminus alters dynamically the coiled-coil structure, with functional implications for the long-range interactions of CtIP with DNA. Our results provide a structural basis for the three-dimensional arrangement of chains in the CtIP tetramer, a key aspect of CtIP function in DNA DSB repair.

PubMed: 34129781
DOI: 10.1098/rsob.210060

Experimental method

X-RAY DIFFRACTION (2.802 Å)