1EVZ

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD

Summary for 1EVZ

• Entry DOI: 10.2210/pdb1evz/pdb
• Related: 1EVY
• Descriptor: GLYCEROL-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PENTADECANE, ... (4 entities in total)
• Functional Keywords: dehydrogenase, rossmann fold, oxidoreductase
• Biological source: Leishmania mexicana
• Cellular location: Glycosome: P90551
• Total number of polymer chains: 1
• Total formula weight: 40193.67

Authors

Suresh, S.,Turley, S.,Opperdoes, F.R.,Michels, P.A.M.,Hol, W.G.J. (deposition date: 2000-04-21, release date: 2001-02-22, Last modification date: 2024-02-07)

Primary citation

Suresh, S.,Turley, S.,Opperdoes, F.R.,Michels, P.A.,Hol, W.G.
A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana.
Structure Fold.Des., 8:541-552, 2000

PubMed Abstract: NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. Although the enzyme has been characterized and cloned from a number of sources, until now no three-dimensional structure has been determined for this enzyme. Although the utility of this enzyme as a drug target against Leishmania mexicana is yet to be established, the critical role played by GPDH in the long slender bloodstream form of the related kinetoplastid Trypanosoma brucei makes it a viable drug target against sleeping sickness.

PubMed: 10801498
DOI: 10.1016/S0969-2126(00)00135-0

Experimental method

X-RAY DIFFRACTION (2.8 Å)