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Structure of Trypanosoma cruzi glycosomal glyceraldehyde‐3‐phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 Å resolution

2002; Wiley; Volume: 520; Issue: 1-3 Linguagem: Inglês

10.1016/s0014-5793(02)02700-x

1873-3468

Fernando Pavão, Marcelo Santos Castilho, Mônica Tallarico Pupo, Raquel Dias, Arlene G. Corrêa, João Batista Fernandes, Maria Fátima das Graças Fernandes da Silva, Jair Mafezoli, Paulo C. Vieira, Glaucius Oliva,

Trypanosoma species research and implications

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 Å 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.