2GGM

Human centrin 2 xeroderma pigmentosum group C protein complex

Summary for 2GGM

• Entry DOI: 10.2210/pdb2ggm/pdb
• Descriptor: Centrin-2, DNA-repair protein complementing XP-C cells, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: ef-hand superfamily, dna repair complex, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole: P41208; Nucleus: Q01831
• Total number of polymer chains: 4
• Total formula weight: 44583.09

Authors

Thompson, J.R. (deposition date: 2006-03-24, release date: 2006-04-25, Last modification date: 2024-10-30)

Primary citation

Thompson, J.R.,Ryan, Z.C.,Salisbury, J.L.,Kumar, R.
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.
J.Biol.Chem., 281:18746-18752, 2006

PubMed Abstract: Human centrin-2 plays a key role in centrosome function and stimulates nucleotide excision repair by binding to the xeroderma pigmentosum group C protein. To determine the structure of human centrin-2 and to develop an understanding of molecular interactions between centrin and xeroderma pigmentosum group C protein, we characterized the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide. Our structure shows that the carboxyl-terminal domain of centrin-2 binds this peptide and two calcium atoms, whereas the amino-terminal lobe is in a closed conformation positioned distantly by an ordered alpha-helical linker. A stretch of the amino-terminal domain unique to centrins appears disordered. Two xeroderma pigmentosum group C peptides both bound to centrin-2 also interact to form an alpha-helical coiled-coil. The interface between centrin-2 and each peptide is predominantly nonpolar, and key hydrophobic residues of XPC have been identified that lead us to propose a novel binding motif for centrin.

PubMed: 16627479
DOI: 10.1074/jbc.M513667200

Experimental method

X-RAY DIFFRACTION (2.35 Å)