1CF2

THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOTHERMUS FERVIDUS

Summary for 1CF2

• Entry DOI: 10.2210/pdb1cf2/pdb
• Descriptor: PROTEIN (GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE), SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: oxydoreductase, oxidoreductase
• Biological source: Methanothermus fervidus
• Cellular location: Cytoplasm: P10618
• Total number of polymer chains: 4
• Total formula weight: 153177.04

Authors

Charron, C.,Talfournier, F.,Isuppov, M.N.,Branlant, G.,Littlechild, J.A.,Vitoux, B.,Aubry, A. (deposition date: 1999-03-24, release date: 2000-03-29, Last modification date: 2023-12-27)

Primary citation

Charron, C.,Talfournier, F.,Isupov, M.N.,Branlant, G.,Littlechild, J.A.,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.,Sect.D, 55:1353-1355, 1999

PubMed Abstract: 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.

PubMed: 10393306
DOI: 10.1107/S0907444999005363

Experimental method

X-RAY DIFFRACTION (2.1 Å)