1FKM

CRYSTAL STRUCTURE OF THE YPT/RAB-GAP DOMAIN OF GYP1P

Summary for 1FKM

• Entry DOI: 10.2210/pdb1fkm/pdb
• Related: 1EK0
• Descriptor: PROTEIN (GYP1P) (2 entities in total)
• Functional Keywords: gap, ypt/rab protein, vesicular trafficking, endocytosis, hydrolase, gtpase activation, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Golgi apparatus, Golgi stack : Q08484
• Total number of polymer chains: 1
• Total formula weight: 47324.64

Authors

Rak, A.,Fedorov, R.,Alexandrov, K.,Albert, S.,Goody, R.S.,Gallwitz, D.,Scheidig, A.J. (deposition date: 2000-08-09, release date: 2001-02-09, Last modification date: 2024-11-06)

Primary citation

Rak, A.,Fedorov, R.,Alexandrov, K.,Albert, S.,Goody, R.S.,Gallwitz, D.,Scheidig, A.J.
Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins.
EMBO J., 19:5105-5113, 2000

PubMed Abstract: We present the 1.9 A 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.

PubMed: 11013213
DOI: 10.1093/emboj/19.19.5105

Experimental method

X-RAY DIFFRACTION (1.9 Å)