3CMC
Thioacylenzyme intermediate of Bacillus stearothermophilus phosphorylating GAPDH
Summary for 3CMC
| Entry DOI | 10.2210/pdb3cmc/pdb |
| Related | 1GD1 1NPT 1NQ5 1NQA 1NQO 2GD1 |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase, SULFATE ION, GLYCERALDEHYDE-3-PHOSPHATE, ... (7 entities in total) |
| Functional Keywords | microspectrophotometry, reaction intermediate, dehydrogenase, phosphate binding site, thioacylenzyme, glycolysis, nad, oxidoreductase |
| Biological source | Bacillus stearothermophilus |
| Cellular location | Cytoplasm: P00362 |
| Total number of polymer chains | 4 |
| Total formula weight | 149826.07 |
| Authors | Moniot, S.,Vonrhein, C.,Bricogne, G.,Didierjean, C.,Corbier, C. (deposition date: 2008-03-21, release date: 2008-06-17, Last modification date: 2024-10-30) |
| Primary citation | Moniot, S.,Bruno, S.,Vonrhein, C.,Didierjean, C.,Boschi-Muller, S.,Vas, M.,Bricogne, G.,Branlant, G.,Mozzarelli, A.,Corbier, C. Trapping of the Thioacylglyceraldehyde-3-phosphate Dehydrogenase Intermediate from Bacillus stearothermophilus: DIRECT EVIDENCE FOR A FLIP-FLOP MECHANISM J.Biol.Chem., 283:21693-21702, 2008 Cited by PubMed Abstract: The crystal structure of the thioacylenzyme intermediate of the phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus has been solved at 1.8A resolution. Formation of the intermediate was obtained by diffusion of the natural substrate within the crystal of the holoenzyme in the absence of inorganic phosphate. To define the soaking conditions suitable for the isolation and accumulation of the intermediate, a microspectrophotometric characterization of the reaction of GAPDH in single crystals was carried out, following NADH formation at 340 nm. When compared with the structure of the Michaelis complex (Didierjean, C., Corbier, C., Fatih, M., Favier, F., Boschi-Muller, S., Branlant, G., and Aubry, A. (2003) J. Biol. Chem. 278, 12968-12976) the 206-210 loop is shifted and now forms part of the so-called "new P(i)" site. The locations of both the O1 atom and the C3-phosphate group of the substrate are also changed. Altogether, the results provide evidence for the flipping of the C3-phosphate group occurring concomitantly or after the redox step. PubMed: 18480053DOI: 10.1074/jbc.M802286200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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