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3KRS

Structure of Triosephosphate Isomerase from Cryptosporidium Parvum at 1.55A Resolution

Summary for 3KRS
Entry DOI10.2210/pdb3krs/pdb
DescriptorTriosephosphate isomerase, SODIUM ION, UNKNOWN ATOM OR ION, ... (4 entities in total)
Functional Keywordsssgcid, sbri, emerald biostructures, university of washington, nih, niaid, triosephosphate isomerase, cryptosporidium parvum, isomerase, structural genomics, seattle structural genomics center for infectious disease
Biological sourceCryptosporidium parvum Iowa II
Total number of polymer chains2
Total formula weight59451.02
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-11-19, release date: 2009-12-01, Last modification date: 2023-09-06)
Primary citationNguyen, T.N.,Abendroth, J.,Leibly, D.J.,Le, K.P.,Guo, W.,Kelley, A.,Stewart, L.,Myler, P.J.,Van Voorhis, W.C.
Structure of triosephosphate isomerase from Cryptosporidium parvum.
Acta Crystallogr.,Sect.F, 67:1095-1099, 2011
Cited by
PubMed 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.
PubMed: 21904056
DOI: 10.1107/S1744309111019178
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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