Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins

Rak, A, Fedorov, R, Alexandrov, K, Albert, S, Goody, RS, Gallwitz, D and Scheidig, AJ (2000) Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins. Embo Journal, 19 19: 5105-5113. doi:10.1093/emboj/19.19.5105


Author Rak, A
Fedorov, R
Alexandrov, K
Albert, S
Goody, RS
Gallwitz, D
Scheidig, AJ
Title Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
Journal name Embo Journal   Check publisher's open access policy
ISSN 0261-4189
Publication date 2000-10-01
Year available 2000
Sub-type Article (original research)
DOI 10.1093/emboj/19.19.5105
Open Access Status Not yet assessed
Volume 19
Issue 19
Start page 5105
End page 5113
Total pages 9
Place of publication OXFORD
Publisher OXFORD UNIV PRESS
Language eng
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.
Keyword GTPase activating protein
Rab protein
vesicular transport
Ypt-GAP domain
Gtpase-Activating Protein
Diffraction Data
Yeast
Transport
Family
Ras
Identification
Prediction
Complex
Member
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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