1JDJ

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH 2-FLUORO-6-CHLOROPURINE

Summary for 1JDJ

• Entry DOI: 10.2210/pdb1jdj/pdb
• Related: 1EVY 1EVZ
• Descriptor: GLYCEROL-3-PHOSPHATE DEHYDROGENASE, 6-CHLORO-2-FLUOROPURINE, PENTADECANE, ... (4 entities in total)
• Functional Keywords: dehydrogenase, oxidoreductase
• Biological source: Leishmania mexicana
• Cellular location: Glycosome : P90551
• Total number of polymer chains: 1
• Total formula weight: 39702.79

Authors

Suresh, S.,Wisedchaisri, G.,Kennedy, K.J.,Verlinde, C.L.M.J.,Gelb, M.H.,Hol, W.G.J. (deposition date: 2001-06-14, release date: 2002-06-14, Last modification date: 2023-08-16)

Primary citation

Choe, J.,Suresh, S.,Wisedchaisri, G.,Kennedy, K.J.,Gelb, M.H.,Hol, W.G.
Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase.
Chem.Biol., 9:1189-1197, 2002

PubMed Abstract: Pathogenic protozoa such as Trypanosome and Leishmania species cause tremendous suffering worldwide. Because of their dependence on glycolysis for energy, the glycolytic enzymes of these organisms, including glycerol-3-phosphate dehydrogenase (GPDH), are considered attractive drug targets. Using the adenine part of NAD as a lead compound, several 2,6-disubstituted purines were synthesized as inhibitors of Leishmania mexicana GPDH (LmGPDH). The electron densities for the inhibitor 2-bromo-6-chloro-purine bound to LmGPDH using a "conventional" wavelength around 1 A displayed a quasisymmetric shape. The anomalous signals from data collected at 1.77 A clearly indicated the positions of the halogen atoms and revealed the multiple binding modes of this inhibitor. Intriguing differences in the observed binding modes of the inhibitor between very similarly prepared crystals illustrate the possibility of crystal-to-crystal variations in protein-ligand complex structures.

PubMed: 12445769
DOI: 10.1016/S1074-5521(02)00243-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)