3krs
From Proteopedia
Structure of Triosephosphate Isomerase from Cryptosporidium Parvum at 1.55A Resolution
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCryptosporidium 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 A 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. Structure of triosephosphate isomerase from Cryptosporidium parvum.,Nguyen TN, Abendroth J, Leibly DJ, Le KP, Guo W, Kelley A, Stewart L, Myler PJ, Van Voorhis WC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1095-9. Epub 2011 Aug 16. PMID:21904056[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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