Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum.
Cryptosporidium parvum is one of the major causes of waterborne diseases worldwide. This protozoan parasite depends mainly on the anaerobic oxidation of glucose for energy production. In order to identify the differences in the three-dimensional structure of key glycolytic enzymes of C. parvum and its human host, we have expressed, purified and crystallized recombinant versions of three important glycolytic enzymes of the parasite, namely, glyceraldehyde 3-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase. Lactate dehydrogenase has been crystallized in the absence and in the presence of its substrates and cofactors, while pyruvate kinase and glyceraldehyde 3-phosphate dehydrogenase were crystallized only in the apo-form. X-ray diffraction data have been collected for all crystals.
Senkovich
Olga
O
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL-35294, USA.
Speed
Haley
H
Grigorian
Alexei
A
Bradley
Kelley
K
Ramarao
Chodavarapu S
CS
Lane
Bessie
B
Zhu
Guan
G
Chattopadhyay
Debasish
D
D000818:Animals; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D016785:Cryptosporidium parvum / Q000201:enzymology* / Q000235:genetics; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006019:Glycolysis; D007770:L-Lactate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011770:Pyruvate Kinase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011770:Pyruvate Kinase