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4LHY

Crystal structure of GDP-bound Rab8:Rabin8

Summary for 4LHY
Entry DOI10.2210/pdb4lhy/pdb
Related4LHV 4LHW 4LHX 4LHZ 4LI0
DescriptorRas-related protein Rab-8A, Rab-3A-interacting protein, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordssmall gtpase, guanine nucleotide exchange factor, protein transport
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Lipid-anchor; Cytoplasmic side (Potential): P61006
Cytoplasm: Q96QF0
Total number of polymer chains6
Total formula weight79430.05
Authors
Guo, Z.,Hou, X.M.,Goody, R.S.,Itzen, A. (deposition date: 2013-07-01, release date: 2013-10-09, Last modification date: 2023-09-20)
Primary citationGuo, Z.,Hou, X.,Goody, R.S.,Itzen, A.
Intermediates in the Guanine Nucleotide Exchange Reaction of Rab8 Protein Catalyzed by Guanine Nucleotide Exchange Factors Rabin8 and GRAB.
J.Biol.Chem., 288:32466-32474, 2013
Cited by
PubMed Abstract: Small G-proteins of the Ras superfamily control the temporal and spatial coordination of intracellular signaling networks by acting as molecular on/off switches. Guanine nucleotide exchange factors (GEFs) regulate the activation of these G-proteins through catalytic replacement of GDP by GTP. During nucleotide exchange, three distinct substrate·enzyme complexes occur: a ternary complex with GDP at the start of the reaction (G-protein·GEF·GDP), an intermediary nucleotide-free binary complex (G-protein·GEF), and a ternary GTP complex after productive G-protein activation (G-protein·GEF·GTP). Here, we show structural snapshots of the full nucleotide exchange reaction sequence together with the G-protein substrates and products using Rabin8/GRAB (GEF) and Rab8 (G-protein) as a model system. Together with a thorough enzymatic characterization, our data provide a detailed view into the mechanism of Rabin8/GRAB-mediated nucleotide exchange.
PubMed: 24072714
DOI: 10.1074/jbc.M113.498329
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227344

數據於2024-11-13公開中

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