1obf: Difference between revisions

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.

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].  

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