1s8f
From Proteopedia
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'''Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II''' | '''Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II''' | ||
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[[Category: Rudolph, M G.]] | [[Category: Rudolph, M G.]] | ||
[[Category: Wittmann, J G.]] | [[Category: Wittmann, J G.]] | ||
| - | [[Category: | + | [[Category: Hemihedral twinning]] |
| - | [[Category: | + | [[Category: Intracellular transport]] |
| - | [[Category: | + | [[Category: Vesicular trafficking]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:25:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:25, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 08:25:27 2008
