Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum

Olga Senkovich, Haley Speed, Alexei Grigorian, Kelley Bradley, Chodavarapu S. Ramarao, Bessie Lane, Guan Zhu, Debasish Chattopadhyay

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)166-172
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1750
Issue number2
DOIs
StatePublished - Jun 30 2005

Keywords

  • Cryptosporidium parvum
  • Crystallization
  • Glyceraldehyde 3-phosphate dehydrogenase
  • Glycolysis
  • Lactate dehydrogenase
  • Pyruvate kinase

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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    Senkovich, O., Speed, H., Grigorian, A., Bradley, K., Ramarao, C. S., Lane, B., Zhu, G., & Chattopadhyay, D. (2005). Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum. Biochimica et Biophysica Acta - Proteins and Proteomics, 1750(2), 166-172. https://doi.org/10.1016/j.bbapap.2005.04.009