PDBsum entry 3rwm

Protein transport

PDB id: 3rwm

Contents

Protein chain

179 a.a.

Ligands

GNP ×2

Metals

_MG

Waters ×192

PDB id:

3rwm

Name:

Protein transport

Title:

Crystal structure of ypt32 in complex with gppnhp

Structure:

Gtp-binding protein ypt32/ypt11. Chain: b. Synonym: rab gtpase ypt32. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: ygl210w, ypt11, ypt32. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.196 R-free: 0.240

Authors:

A.Sultana,C.Dregger,Y.Jin,E.Franklin,L.S.Weisman,A.R.Khan

Key ref:

A.Sultana et al. (2011). The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding. Febs Lett, 585, 3520-3527. PubMed id: 22024479

Date:

09-May-11 Release date: 26-Oct-11

Protein chain

P51996  (YPT32_YEAST) -  GTP-binding protein YPT32/YPT11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 222 a.a.

Struc: 179 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Febs Lett 585:3520-3527 (2011)

PubMed id: 22024479

The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding.

A.Sultana, Y.Jin, C.Dregger, E.Franklin, L.S.Weisman, A.R.Khan.

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.