1KY3

GDP-BOUND YPT7P AT 1.35 A RESOLUTION

Summary for 1KY3

• Entry DOI: 10.2210/pdb1ky3/pdb
• Related: 1KY2
• Descriptor: GTP-BINDING PROTEIN YPT7P, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: g protein, vesicular traffic, gtp hydrolysis, ypt/rab protein, endocytosis, hydrolase, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Vacuole: P32939
• Total number of polymer chains: 1
• Total formula weight: 20627.27

Authors

Constantinescu, A.-T.,Rak, A.,Scheidig, A.J. (deposition date: 2002-02-02, release date: 2002-06-05, Last modification date: 2024-04-03)

Primary citation

Constantinescu, A.T.,Rak, A.,Alexandrov, K.,Esters, H.,Goody, R.S.,Scheidig, A.J.
Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases.
Structure, 10:569-579, 2002

PubMed Abstract: The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 A resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope. Ypt7p*GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins.

PubMed: 11937061
DOI: 10.1016/S0969-2126(02)00737-2

Experimental method

X-RAY DIFFRACTION (1.35 Å)