1obf

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|PDB= 1obf |SIZE=350|CAPTION= <scene name='initialview01'>1obf</scene>, resolution 1.7&Aring;
|PDB= 1obf |SIZE=350|CAPTION= <scene name='initialview01'>1obf</scene>, resolution 1.7&Aring;
|SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+P'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+P'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene>
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|LIGAND= <scene name='pdbligand=CSW:CYSTEINE-S-DIOXIDE'>CSW</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1obf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obf OCA], [http://www.ebi.ac.uk/pdbsum/1obf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1obf RCSB]</span>
}}
}}
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[[Category: Hasnain, S S.]]
[[Category: Hasnain, S S.]]
[[Category: Strange, R W.]]
[[Category: Strange, R W.]]
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[[Category: K]]
 
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[[Category: PG4]]
 
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[[Category: SO4]]
 
[[Category: free-nad gapdh]]
[[Category: free-nad gapdh]]
[[Category: glycolytic pathway]]
[[Category: glycolytic pathway]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:43 2008''

Revision as of 19:42, 30 March 2008


PDB ID 1obf

Drag the structure with the mouse to rotate
, resolution 1.7Å
Sites:
Ligands: , , ,
Activity: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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