3RWO

Crystal structure of YPT32 in complex with GDP

Summary for 3RWO

• Entry DOI: 10.2210/pdb3rwo/pdb
• Related: 3RWM
• Descriptor: GTP-binding protein YPT32/YPT11, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: gtpases, protein-gdp complex, exocytosis, golgi apparatus, gtp-binding, lipoprotein, membrane, nucleotide-binding, prenylation, protein transport, transport, ypt32, rab gtpase, gdp, vesicle trafficking, myo2p, effectors
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Golgi apparatus membrane; Lipid-anchor: P51996
• Total number of polymer chains: 2
• Total formula weight: 42141.14

Authors

Sultana, A.,Jin, Y.,Dregger, C.,Franklin, E.,Weisman, L.S.,Khan, A.R. (deposition date: 2011-05-09, release date: 2011-10-26, Last modification date: 2023-09-13)

Primary citation

Sultana, A.,Jin, Y.,Dregger, C.,Franklin, E.,Weisman, L.S.,Khan, A.R.
The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding.
Febs Lett., 585:3520-3527, 2011

PubMed Abstract: Rab GTPases localize to distinct sub-cellular compartments and regulate vesicle trafficking in eukaryotic cells. Yeast Rabs Ypt31/32 and Sec4 have 68% homology and bind to common interactors, yet play distinct roles in the transport of exocytic vesicles. The structures of Ypt31/32 have not previously been reported in the uncomplexed state. We describe the crystal structures of GTP and GDP forms of Ypt32 to understand the molecular basis for Rab function. The structure of Ypt32(GTP) reveals that the switch II conformation is distinct from Sec4(GTP) in spite of a highly conserved amino acid sequence. Also, Ypt32(GDP) reveals a remarkable change in conformation of the switch II helix induced by binding to GDI, which has not been described previously.

PubMed: 22024479
DOI: 10.1016/j.febslet.2011.10.013

Experimental method

X-RAY DIFFRACTION (1.7 Å)