title: Structure of triosephosphate isomerase from Cryptosporidium parvum.
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.
authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
authors: Trang N
authors: TN
authors: Nguyen
authors: Jan
authors: J
authors: Abendroth
authors: David J
authors: DJ
authors: Leibly
authors: Kristen P
authors: KP
authors: Le
authors: Wenjin
authors: W
authors: Guo
authors: Angela
authors: A
authors: Kelley
authors: Lance
authors: L
authors: Stewart
authors: Peter J
authors: PJ
authors: Myler
authors: Wesley C
authors: WC
authors: Van Voorhis
mesh_terms: D020134:Catalytic Domain; D016785:Cryptosporidium parvum / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*
chemical_list: D014305:Triose-Phosphate Isomerase