Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of glyoxalase I from Leishmania infantum

• Tipo: Artigo em Revista Científica Internacional
• Data: 2010

Autores

barata, l (Autor) Outra; silva, ms (Autor) Outra; schuldt, l (Autor) Outra; da costa, g (Autor) Outra; tomas, am (Autor) FCUP; ferreira, aen (Autor) Outra; weiss, ms (Autor) Outra; freire, ap (Autor) Outra; cordeiro, c (Autor) Outra

Revista

Título: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Vol. 66

Páginas: 571-574

ISSN: 1744-3091

Editora: John Wiley & Sons

Indexação

ISI Web of Knowledge - 6 Citações

Scopus - 6 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-003-6SS

DOI: 10.1107/S1744309110010754

Abstract (EN): Glyoxalase I (GLO1) is the first of the two glyoxalase-pathway enzymes. It catalyzes the formation of S-D-lactoyltrypanothione from the non-enzymatically formed hemithioacetal of methylglyoxal and reduced trypanothione. In order to understand its substrate binding and catalytic mechanism, GLO1 from Leishmania infantum was cloned, overexpressed in Escherichia coli, purified and crystallized. Two crystal forms were obtained: a cube-shaped form and a rod-shaped form. While the cube-shaped form did not diffract X-rays at all, the rod-shaped form exhibited diffraction to about 2.0 angstrom resolution. The crystals belonged to space group P21212, with unit-cell parameters a = 130.03, b = 148.51, c = 50.63 angstrom and three dimers of the enzyme per asymmetric unit.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 4