Structural highlights
Function
[G3P_METFE] Exhibits a dual-cofactor specificity, with a marked preference for NADP(+) over NAD(+).[HAMAP-Rule:MF_00559]
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 homotetrameric holo-D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized in the presence of NADP+ using the hanging-drop vapour-diffusion method. Crystals grew from a solution containing 2-methyl-2,4-pentanediol and magnesium acetate. A native data set has been collected to 2.1 A using synchrotron radiation and cryocooling. Diffraction data have been processed in the orthorhombic system (space group P21212) with unit-cell dimensions a = 136.7, b = 153.3, c = 74.9 A and one tetramer per asymmetric unit.
Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus.,Charron C, Talfournier F, Isupov MN, Branlant G, Littlechild JA, Vitoux B, Aubry A Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1353-5. PMID:10393306[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Charron C, Talfournier F, Isupov MN, Branlant G, Littlechild JA, Vitoux B, Aubry A. Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus. Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1353-5. PMID:10393306
