1K3T

Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi Complexed with Chalepin, a Coumarin Derivative Inhibitor

Summary for 1K3T

• Entry DOI: 10.2210/pdb1k3t/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase, 6-(1,1-DIMETHYLALLYL)-2-(1-HYDROXY-1-METHYLETHYL)-2,3-DIHYDRO-7H-FURO[3,2-G]CHROMEN-7-ONE (3 entities in total)
• Functional Keywords: apo-protein, ggapdh-chalepin complex, glycosome, trypanosoma cruzi, oxidoreductase
• Biological source: Trypanosoma cruzi
• Cellular location: Glycosome: P22513
• Total number of polymer chains: 4
• Total formula weight: 156764.53

Authors

Pavao, F. (deposition date: 2001-10-04, release date: 2002-06-19, Last modification date: 2024-12-25)

Primary citation

Pavao, F.,Castilho, M.S.,Pupo, M.T.,Dias, R.L.,Correa, A.G.,Fernandes, J.B.,da Silva, M.F.,Mafezoli, J.,Vieira, P.C.,Oliva, G.
Structure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 A resolution.
FEBS Lett., 520:13-17, 2002

PubMed Abstract: The structure of the glycosomal glyceraldehyde-3-phosphate dehydrogenase (gGAPDH) from Trypanosoma cruzi complexed with chalepin, a natural product from Pilocarpus spicatus, has been determined by X-ray crystallography to 1.95 A resolution. The structure is in the apo form without cofactors in the subunits of the tetrameric gGAPDH in the asymmetric unit. Unequivocal density corresponding to the inhibitor was clearly identified in one monomer. The final refined model of the complex shows extensive conformational changes when compared with the native structure. The mode of binding of chalepin to gGAPDH and its implications for inhibitor design are discussed.

PubMed: 12044862
DOI: 10.1016/S0014-5793(02)02700-X

Experimental method

X-RAY DIFFRACTION (1.95 Å)