Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition
Authors: Cordeiro, Artur T.; Hardré, Renaud; Michels, Paul A. M.; Salmon, Laurent; Delboni, Luis F.; Thiemann, Otavio H.
Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 915-919(5)
Publisher: Blackwell Publishing
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Abstract:
Glucose-6-phosphate isomerase (PGI; EC 5.3.1.9; also often called by its old nomenclature phosphoglucose isomerase) is an intracellular enzyme that catalyses the reversible conversion ofd-glucose 6-phosphate (G6P) tod-fructose 6-phosphate (F6P). The native Leishmania PGI is a homodimeric molecule of 60 kDa per monomer with 47% sequence identity to human PGI. It has been shown to be present in both the cytosol and the glycosome of Leishmania promastigotes and represents a potential target for rational drug design. The present work describes the crystallization of two bacterially expressed Leishmania PGI constructs, one corresponding to the natural protein and the other to an N-terminally deleted form. Crystals of both forms are identical and present a large c unit-cell parameter. A complete data set was collected from the N-terminally deleted PGI to a resolution of 3.3 Å in space group P61, with unit-cell parameters a = b = 87.0, c = 354.7 Å, α = β = 90, γ = 120°. A preliminary study of the first inhibitors to be evaluated on the Leishmania enzyme is also reported.Keywords: glycosome; Leishmania mexicana mexicana; glucose-6-phosphate isomerase; sugar phosphates
Document Type: Research article
DOI: 10.1107/S0907444904003762
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