2X0N

Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data

Replaces:  1GGA

Summary for 2X0N

• Entry DOI: 10.2210/pdb2x0n/pdb
• Descriptor: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, GLYCOSOMAL, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: glycolysis, glycosome, oxidoreductase
• Biological source: TRYPANOSOMA BRUCEI BRUCEI
• Cellular location: Glycosome: P22512
• Total number of polymer chains: 6
• Total formula weight: 239683.24

Authors

Vellieux, F.M.D.,Hajdu, J.,Hol, W.G.J. (deposition date: 2009-12-16, release date: 2009-12-22, Last modification date: 2023-12-20)

Primary citation

Vellieux, F.M.D.,Hajdu, J.,Verlinde, C.L.,Groendijk, H.,Read, R.J.,Greenhough, T.J.,Campbell, J.W.,Kalk, K.H.,Littlechild, J.A.,Watson, H.C.
Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma Brucei Determined from Laue Data.
Proc.Natl.Acad.Sci.USA, 90:2355-, 1993

PubMed Abstract: The three-dimensional structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase [D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.12.1.12] from the sleeping-sickness parasite Trypanosoma brucei was solved by molecular replacement at 3.2-A resolution with an x-ray data set collected by the Laue method. For data collection, three crystals were exposed to the polychromatic synchrotron x-ray beam for a total of 20.5 sec. The structure was solved by using the Bacillus stearothermophilus enzyme model [Skarzyński, T., Moody, P. C. E. & Wonacott, A. J. (1987) J. Mol. Biol. 193, 171-187] with a partial data set which was 37% complete. The crystals contain six subunits per asymmetric unit, which allowed us to overcome the absence of > 60% of the reflections by 6-fold density averaging. After molecular dynamics refinement, the current molecular model has an R factor of 17.6%. Comparing the structure of the trypanosome enzyme with that of the homologous human muscle enzyme, which was determined at 2.4-A resolution, reveals important structural differences in the NAD binding region. These are of great interest for the design of specific inhibitors of the parasite enzyme.

PubMed: 8460146
DOI: 10.1073/PNAS.90.6.2355

Experimental method

X-RAY DIFFRACTION (3.2 Å)