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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 9(67), p. 1095-1099, 2011

DOI: 10.1107/s1744309111019178

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Structure of triosephosphate isomerase fromCryptosporidium parvum

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.