1B7G

GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE

Summary for 1B7G

• Entry DOI: 10.2210/pdb1b7g/pdb
• Descriptor: PROTEIN (GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE), SULFATE ION (3 entities in total)
• Functional Keywords: archaea; hyperthermophile; gapdh; hyperthermophilic dehydrogenase, oxidoreductase
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm: P39460
• Total number of polymer chains: 2
• Total formula weight: 76415.99

Authors

Isupov, M.N.,Littlechild, J.A. (deposition date: 1999-01-22, release date: 1999-10-08, Last modification date: 2024-10-30)

Primary citation

Isupov, M.N.,Fleming, T.M.,Dalby, A.R.,Crowhurst, G.S.,Bourne, P.C.,Littlechild, J.A.
Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
J.Mol.Biol., 291:651-660, 1999

PubMed Abstract: 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.

PubMed: 10448043
DOI: 10.1006/jmbi.1999.3003

Experimental method

X-RAY DIFFRACTION (2.05 Å)