1obf: Difference between revisions

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[[Image:1obf.gif|left|200px]]
{{Seed}}
[[Image:1obf.png|left|200px]]


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{{STRUCTURE_1obf|  PDB=1obf  |  SCENE=  }}  
{{STRUCTURE_1obf|  PDB=1obf  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ALCALIGENES XYLOSOXIDANS AT 1.7 RESOLUTION.'''
===THE CRYSTAL STRUCTURE OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ALCALIGENES XYLOSOXIDANS AT 1.7 RESOLUTION.===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_12777799}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12777799}}


==About this Structure==
==About this Structure==
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[[Category: Glycolytic pathway]]
[[Category: Glycolytic pathway]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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