1s8f
Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch IICrystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
Structural highlights
Function[RAB9A_CANFA] Involved in the transport of proteins between the endosomes and the trans-Golgi network. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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