TY - JOUR
T1 - Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum
AU - Senkovich, Olga
AU - Speed, Haley
AU - Grigorian, Alexei
AU - Bradley, Kelley
AU - Ramarao, Chodavarapu S.
AU - Lane, Bessie
AU - Zhu, Guan
AU - Chattopadhyay, Debasish
N1 - Funding Information:
C. parvum cDNA was obtained from NIH AIDS Reagents Program. This work was supported by a research grant (106493-35-RGGN from American Foundation for AIDS Research, amfAR). We thank the staff of the SBC-CAT beam line at APS for their assistance during data collection.
PY - 2005/6/30
Y1 - 2005/6/30
N2 - 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.
AB - 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.
KW - Cryptosporidium parvum
KW - Crystallization
KW - Glyceraldehyde 3-phosphate dehydrogenase
KW - Glycolysis
KW - Lactate dehydrogenase
KW - Pyruvate kinase
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U2 - 10.1016/j.bbapap.2005.04.009
DO - 10.1016/j.bbapap.2005.04.009
M3 - Article
C2 - 15953771
AN - SCOPUS:20644454388
SN - 1570-9639
VL - 1750
SP - 166
EP - 172
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 2
ER -