1b7g

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File:1b7g.jpg


1b7g, resolution 2.05Å

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GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE

OverviewOverview

The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond.

About this StructureAbout this Structure

1B7G is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus., Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA, J Mol Biol. 1999 Aug 20;291(3):651-60. PMID:10448043

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