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Titolo:
CRYSTAL-STRUCTURE OF THE CELL CYCLE-REGULATORY PROTEIN SUC1 REVEALS ABETA-HINGE CONFORMATIONAL SWITCH
Autore:
BOURNE Y; ARVAI AS; BERNSTEIN SL; WATSON MH; REED SI; ENDICOTT JE; NOBLE ME; JOHNSON LN; TAINER JA;
Indirizzi:
SCRIPPS CLIN & RES INST,MB4,10666 N TORREY PINES RD LA JOLLA CA 92037 UNIV OXFORD,MOLEC BIOPHYS LAB OXFORD OX1 3QU ENGLAND CNRS,INST FERERAT RECH CONCERTEE 1,CRISTALLISAT & CRISTALLISAT MACROMOLECULES BIOL L F-13402 MARSEILLE 20 FRANCE
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 22, volume: 92, anno: 1995,
pagine: 10232 - 10236
SICI:
0027-8424(1995)92:22<10232:COTCCP>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
SCHIZOSACCHAROMYCES-POMBE; SACCHAROMYCES-CEREVISIAE; FISSION YEAST; PROMOTING FACTOR; CDC2 PROTEIN; KINASE; COMPLEX; GENE; ACTIVATION; SUPPRESSES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
Y. Bourne et al., "CRYSTAL-STRUCTURE OF THE CELL CYCLE-REGULATORY PROTEIN SUC1 REVEALS ABETA-HINGE CONFORMATIONAL SWITCH", Proceedings of the National Academy of Sciences of the United Statesof America, 92(22), 1995, pp. 10232-10236

Abstract

The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-functionrelationships and to help resolve conflicting interpretations of suc1function based on genetic studies of suc1 and its functional homologsin both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer, Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits, This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here, This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs tothe family of domain-swapping proteins, consisting of intertwined anddimeric protein structures in which the dual assembly modes regulate their function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 21:18:56