1OBF
The crystal structure of Glyceraldehyde 3-phosphate Dehydrogenase from Alcaligenes xylosoxidans at 1.7A resolution.
Summary for 1OBF
| Entry DOI | 10.2210/pdb1obf/pdb |
| Descriptor | GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, SULFATE ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | glycolytic pathway, oxidoreductase, free-nad gapdh |
| Biological source | ACHROMOBACTER XYLOSOXIDANS (ALCALIGENES XYLOSOXIDANS) |
| Total number of polymer chains | 2 |
| Total formula weight | 72217.49 |
| Authors | Antonyuk, S.V.,Eady, R.R.,Strange, R.W.,Hasnain, S.S. (deposition date: 2003-01-30, release date: 2003-06-12, Last modification date: 2023-12-13) |
| Primary citation | Antonyuk, S.V.,Eady, R.R.,Strange, R.W.,Hasnain, S.S. The Structure of Glyceraldehyde 3-Phosphate Dehydrogenase from Alcaligenes Xylosoxidans at 1.7 A Resolution Acta Crystallogr.,Sect.D, 59:835-, 2003 Cited by PubMed Abstract: The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the Gram-negative denitrifying bacterial species Alcaligenes xylosoxidans was purified and crystallized as a contaminant protein during purification of nitrous oxide reductase. This is the first structure of a GAPDH from a denitrifying species. The crystal structure was solved at 1.7 A resolution by molecular replacement using the structure of GAPDH from Bacillus stearothermophilus as a starting model. The quality of the structure enabled the amino-acid sequence of the A. xylosoxidans GAPDH to be assigned. The structure is that of the apo-enzyme, lacking the NAD+ cofactor and with the active-site residue Cys154 oxidized. The global structure of the enzyme has a homotetrameric quaternary structure similar to that observed for its bacterial and eukaryotic counterparts. The essential role of Cys154 in the enzyme activity has been confirmed. In monomer O two half-occupancy sulfate ions were found at the active site, which are analogous to the substrate and the "attacking" phosphate seen in B. stearothermophilus. One half-occupancy sulfate ion is also located in the substrate-binding site of monomer P. PubMed: 12777799DOI: 10.1107/S0907444903041441 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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