1s8f
Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
OverviewOverview
The small GTPase Rab9 is an essential regulator of vesicular transport from the late endosome to the trans-Golgi network, as monitored by the redirection of the mannose-6-phosphate receptors. The crystal structure of Rab9 complexed to GDP, Mg(2+), and Sr(2+) reveals a unique dimer formed by an intermolecular beta-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9 . GDP that is independent of GDI. Mg(2+)-bound Rab9 represents an inactive state, but Sr(2+)-bound Rab9 . GDP displays activated switch region conformations, mimicking those of the GTP state. A hydrophobic tetrad is formed resembling an effector-discriminating epitope found only in GTP-bound Rab proteins.
About this StructureAbout this Structure
1S8F is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II., Wittmann JG, Rudolph MG, FEBS Lett. 2004 Jun 18;568(1-3):23-9. PMID:15196914 Page seeded by OCA on Sat May 3 08:25:27 2008