1s8f | pdb_00001s8f
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Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
Overview
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 Structure
1S8F is a Single protein structure of sequence from Canis lupus familiaris with SR, MG, CL, GDP and BEZ as ligands. Full crystallographic information is available from OCA.
Reference
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
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