Structural highlights
Function
[G3P_SULSO] Can use both NAD and NADP as cofactors, but exhibits a marked preference for NADP.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA. Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J Mol Biol. 1999 Aug 20;291(3):651-60. PMID:10448043 doi:10.1006/jmbi.1999.3003
