1A12

REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN

Summary for 1A12

• Entry DOI: 10.2210/pdb1a12/pdb
• Descriptor: REGULATOR OF CHROMOSOME CONDENSATION 1 (2 entities in total)
• Functional Keywords: guanine nucleotide exchange factor, gef, ran, ras-like nuclear gtp binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 132329.33

Authors

Renault, L.,Nassar, N.,Vetter, I.,Becker, J.,Roth, M.,Wittinghofer, A. (deposition date: 1997-12-19, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

Renault, L.,Nassar, N.,Vetter, I.,Becker, J.,Klebe, C.,Roth, M.,Wittinghofer, A.
The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller.
Nature, 392:97-101, 1998

PubMed Abstract: The gene encoding the regulator of chromosome condensation (RCC1) was cloned by virtue of its ability to complement the temperature-sensitive phenotype of the hamster cell line tsBN2, which undergoes premature chromosome condensation or arrest in the G1 phase of the cell cycle at non-permissive temperatures. RCC1 homologues have been identified in many eukaryotes, including budding and fission yeast. Mutations in the gene affect pre-messenger RNA processing and transport, mating, initiation of mitosis and chromatin decondensation, suggesting that RCC1 is important in the control of nucleo-cytoplasmic transport and the cell cycle. Biochemically, RCC1 is a guanine-nucleotide-exchange factor for the nuclear Ras homologue Ran; it increases the dissociation of Ran-bound GDP by 10(5)-fold. It may also bind to DNAvia a protein-protein complex. Here we show that the structure of human RCC1, solved to 1.7-A resolution by X-ray crystallography, consists of a seven-bladed propeller formed from internal repeats of 51-68 residues per blade. The sequence and structure of the repeats differ from those of WD40-domain proteins, which also form seven-bladed propellers and include the beta-subunits of G proteins. The nature of the structure explains the consequences of a wide range of known mutations. The region of the protein that is involved in guanine-nucleotide exchange is located opposite the region that is thought to be involved in chromosome binding.

PubMed: 9510255
DOI: 10.1038/32204

Experimental method

X-RAY DIFFRACTION (1.7 Å)