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2EFC

Ara7-GDP/AtVps9a

Summary for 2EFC
Entry DOI10.2210/pdb2efc/pdb
Related2efe 2efh 2fed
DescriptorSimilarity to vacuolar protein sorting-associated protein VPS9, Small GTP-binding protein-like, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsgef, gtpase, vps9, rab5, nucleotide, transport protein
Biological sourceArabidopsis thaliana (thale cress)
More
Cellular locationEarly endosome membrane: Q9SN68
Total number of polymer chains4
Total formula weight100997.90
Authors
Uejima, T.,Ihara, K.,Goh, T.,Ito, E.,Sunada, M.,Ueda, T.,Nakano, A.,Wakatsuki, S. (deposition date: 2007-02-22, release date: 2008-02-26, Last modification date: 2024-04-03)
Primary citationUejima, T.,Ihara, K.,Goh, T.,Ito, E.,Sunada, M.,Ueda, T.,Nakano, A.,Wakatsuki, S.
GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5/Vps9 system
J.Biol.Chem., 285:36689-36697, 2010
Cited by
PubMed Abstract: Many GTPases regulate intracellular transport and signaling in eukaryotes. Guanine nucleotide exchange factors (GEFs) activate GTPases by catalyzing the exchange of their GDP for GTP. Here we present crystallographic and biochemical studies of a GEF reaction with four crystal structures of Arabidopsis thaliana ARA7, a plant homolog of Rab5 GTPase, in complex with its GEF, VPS9a, in the nucleotide-free and GDP-bound forms, as well as a complex with aminophosphonic acid-guanylate ester and ARA7·VPS9a(D185N) with GDP. Upon complex formation with ARA7, VPS9 wedges into the interswitch region of ARA7, inhibiting the coordination of Mg(2+) and decreasing the stability of GDP binding. The aspartate finger of VPS9a recognizes GDP β-phosphate directly and pulls the P-loop lysine of ARA7 away from GDP β-phosphate toward switch II to further destabilize GDP for its release during the transition from the GDP-bound to nucleotide-free intermediates in the nucleotide exchange reaction.
PubMed: 20833725
DOI: 10.1074/jbc.M110.152132
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.09 Å)
Structure validation

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건을2025-06-11부터공개중

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