You are here

Structure of triosephosphate isomerase from Cryptosporidium parvum.

TitleStructure of triosephosphate isomerase from Cryptosporidium parvum.
Publication TypeJournal Article
Year of Publication2011
AuthorsNguyen, TN, Abendroth, J, Leibly, DJ, Le, KP, Guo, W, Kelley, A, Stewart, L, Myler, PJ, Van Voorhis, WC
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume67
IssuePt 9
Pagination1095-9
Date Published2011 Sep 1
ISSN1744-3091
KeywordsCatalytic Domain, Cryptosporidium parvum, Crystallography, X-Ray, Models, Molecular, Protein Structure, Quaternary, Triose-Phosphate Isomerase
Abstract

Cryptosporidium parvum is one of several Cryptosporidium spp. that cause the parasitic infection cryptosporidiosis. Cryptosporidiosis is a diarrheal infection that is spread via the fecal-oral route and is commonly caused by contaminated drinking water. Triosephosphate isomerase is an enzyme that is ubiquitous to all organisms that perform glycolysis. Triosephosphate isomerase catalyzes the formation of glyceraldehyde 3-phosphate from dihydroxyacetone phosphate, which is a critical step to ensure the maximum ATP production per glucose molecule. In this paper, the 1.55 Å resolution crystal structure of the open-loop form of triosephosphate isomerase from C. parvum Iowa II is presented. An unidentified electron density was found in the active site.

DOI10.1107/S1744309111019178
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID21904056