4LI0
Crystal structure of GDP-bound Rab8:GRAB
Summary for 4LI0
Entry DOI | 10.2210/pdb4li0/pdb |
Related | 4LHV 4LHW 4LHX 4LHY 4LHZ |
Descriptor | Ras-related protein Rab-8A, Guanine nucleotide exchange factor for Rab-3A, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | small gtpase, guanine nucleotide exchange factor, protein transport |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P61006 |
Total number of polymer chains | 6 |
Total formula weight | 82605.69 |
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 citation | Guo, 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: 24072714DOI: 10.1074/jbc.M113.498329 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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