1obf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 ... | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OBF is a | + | 1OBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans] with SO4, K and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:04:17 2007'' |
Revision as of 10:58, 5 November 2007
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THE CRYSTAL STRUCTURE OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ALCALIGENES XYLOSOXIDANS AT 1.7 RESOLUTION.
Overview
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.
About this Structure
1OBF is a Single protein structure of sequence from Achromobacter xylosoxidans with SO4, K and PG4 as ligands. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The structure of glyceraldehyde 3-phosphate dehydrogenase from Alcaligenes xylosoxidans at 1.7 A resolution., Antonyuk SV, Eady RR, Strange RW, Hasnain SS, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):835-42. Epub 2003, Apr 25. PMID:12777799
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