1S8F

Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II

Summary for 1S8F

• Entry DOI: 10.2210/pdb1s8f/pdb
• Descriptor: Ras-related protein Rab-9A, STRONTIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: intracellular transport, vesicular trafficking, hemihedral twinning, protein transport
• Biological source: Canis lupus familiaris (dog)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P24408
• Total number of polymer chains: 2
• Total formula weight: 41684.68

Authors

Wittmann, J.G.,Rudolph, M.G. (deposition date: 2004-02-02, release date: 2004-06-11, Last modification date: 2023-08-23)

Primary citation

Wittmann, J.G.,Rudolph, M.G.
Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II.
Febs Lett., 568:23-29, 2004

PubMed Abstract: 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.

PubMed: 15196914
DOI: 10.1016/j.febslet.2004.05.004

Experimental method

X-RAY DIFFRACTION (1.77 Å)