Literature DB >> 15953771

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

Olga Senkovich1, Haley Speed, Alexei Grigorian, Kelley Bradley, Chodavarapu S Ramarao, Bessie Lane, Guan Zhu, Debasish Chattopadhyay.   

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.

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Year:  2005        PMID: 15953771     DOI: 10.1016/j.bbapap.2005.04.009

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Crystal structure of Cryptosporidium parvum pyruvate kinase.

Authors:  William J Cook; Olga Senkovich; Khadijah Aleem; Debasish Chattopadhyay
Journal:  PLoS One       Date:  2012-10-09       Impact factor: 3.240

2.  An unexpected phosphate binding site in glyceraldehyde 3-phosphate dehydrogenase: crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme.

Authors:  William J Cook; Olga Senkovich; Debasish Chattopadhyay
Journal:  BMC Struct Biol       Date:  2009-02-25
  2 in total

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