TY - JOUR
T1 - Purification, crystallization and preliminary X-ray diffraction analysis of the glyoxalase II from Leishmania infantum
AU - Barata, Lauro Euclides Soares
AU - Silva, Marta Sousa
AU - Trincão, José Pedro da Silva
AU - Carvalho, Sandra
AU - Ferreira, António Eduardo N.
AU - Bonifácio, Cecília S.
AU - Cordeiro, Carlos
AU - Tomás, Ana M.
AU - Freire, Ana Ponces
AU - Romão, Maria João
PY - 2006/8
Y1 - 2006/8
N2 - 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.
AB - 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.
U2 - 10.1107/S1744309106027539
DO - 10.1107/S1744309106027539
M3 - Article
C2 - 16880563
SN - 1744-3091
VL - 62
SP - 805
EP - 807
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 8
ER -