1b7g

Revision as of 12:18, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1b7g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7g, resolution 2.05Å" /> '''GLYCERALDEHYDE 3-PHO...)
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GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE

File:1b7g.jpg


1b7g, resolution 2.05Å

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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 SO4 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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