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Titolo:
Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
Autore:
Rak, A; Fedorov, R; Alexandrov, K; Albert, S; Goody, RS; Gallwitz, D; Scheidig, AJ;
Indirizzi:
Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44227 Dortmund, Germany Max Planck Inst Mol Physiol Dortmund Germany D-44227 7 Dortmund, Germany Max Planck Inst Biophys Chem, Dept Mol Genet, D-37070 Gottingen, Germany Max Planck Inst Biophys Chem Gottingen Germany D-37070 ottingen, Germany
Titolo Testata:
EMBO JOURNAL
fascicolo: 19, volume: 19, anno: 2000,
pagine: 5105 - 5113
SICI:
0261-4189(20001002)19:19<5105:CSOTGD>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; DIFFRACTION DATA; YEAST; TRANSPORT; FAMILY; RAS; IDENTIFICATION; PREDICTION; COMPLEX; MEMBER;
Keywords:
GTPase activating protein; Rab protein; vesicular transport; Ypt-GAP domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Scheidig, AJ Max Planck Inst Mol Physiol, Dept Phys Biochem, Otto Hahn Str11, D-44227 Dortmund, Germany Max Planck Inst Mol Physiol Otto Hahn Str 11Dortmund Germany D-44227
Citazione:
A. Rak et al., "Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins", EMBO J, 19(19), 2000, pp. 5105-5113

Abstract

We present the 1.9 Angstrom resolution crystal structure of the catalytic domain of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the yeast homologues of Rab proteins, which are involved in vesicular transport. Gyp1p is a member of a large family of eukaryotic proteins with shared sequence motifs, Previously, no structural information was available for any member of this class of proteins. The GAP domain of Gyp1p was found to be fully alpha-helical. However, the observed fold does not superimpose with other alpha-helical GAPs (e.g. Ras- and Cdc42/Rho-GAP), The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs, A model for the interaction between Gyp1p and the Ypt protein satisfying biochemical data is given.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:32:27