Purification, crystallization and preliminary X-ray diffraction analysis of the glyoxalase II from Leishmania infantum

Lauro Euclides Soares Barata, Marta Sousa Silva, José Pedro da Silva Trincão, Sandra Carvalho, António Eduardo N. Ferreira, Cecília S. Bonifácio, Carlos Cordeiro, Ana M. Tomás, Ana Ponces Freire, Maria João Romão

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4 Citations (Scopus)
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Abstract

In trypanosomatids, trypanothione replaces glutathione in all glutathione-dependent processes. Of the two enzymes involved in the glyoxalase pathway, glyoxalase I and glyoxalase II, the latter shows absolute specificity towards trypanothione thioester, making this enzyme an excellent model to understand the molecular basis of trypanothione binding. Cloned glyoxalase II from Leishmania infantum was overexpressed in Escherichia coli, purified and crystallized. Crystals belong to space group C222(1) (unit-cell parameters a = 65.6, b = 88.3, c = 85.2 angstrom) and diffract beyond 2.15 angstrom using synchrotron radiation. The structure was solved by molecular replacement using the human glyoxalase II structure as a search model. These results, together with future detailed kinetic characterization using lactoyltrypanothione, should shed light on the evolutionary selection of trypanothione instead of glutathione by trypanosomatids.
Original languageEnglish
Pages (from-to)805-807
JournalActa Crystallographica Section F-Structural Biology And Crystallization Com
Volume62
Issue number8
DOIs
Publication statusPublished - Aug 2006

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