The taxonomic range for the selected organisms is: Cryptosporidium parvum The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
each monomer in the asymmetric unit of CpPyK binds two sulfate ions at equivalent positions, one in the C-domain and the other at the interface of the A and C domains, binding structure, overview. The sulfate ion in the C-domain occupies a position corresponding to the 6-phosphate of the effector molecule in different PyKs
pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules, mainly phosphosugars, due to blockage of the effector binding site by a sulfate ion, overview
the partially closed active site structure contains an alpha6' helix that unwinds and assumes an extended conformation, a glycerol molecule is located near the gamma-phosphate site of ATP. A sulfate ion is found at a site that is occupied by a phosphate of the effector molecule
the partially closed active site structure contains an alpha6' helix that unwinds and assumes an extended conformation, a glycerol molecule is located near the gamma-phosphate site of ATP. A sulfate ion is found at a site that is occupied by a phosphate of the effector molecule
three-dimensional structure determination and analysis, structure comparisons, overview. Each CpPyK monomer consists of four domains: N (residues 23-32), A (residues 42-112 and 212-389), B (residues 113-211) and C (residues 390-526). The A-domain constitutes the central part of the molecule and forms a parallel (alphaa/beta)8 barrel. The B-domain contains nine beta strands that form an antiparallel beta-barrel. The active site is located at the interface of the A and B domains, and residues from both domains participate in substrate binding. The C-domain is composed of five beta strands surrounded by five alpha-helices. The allosteric site for binding the effector molecule is located in the C-domain. The A domains of the two monomers A and B form the major interface
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant untagged enzyme in apoform or complexed with the non-hydrolyzable ATP analogue adenyl-5'-yl imidodiphosphate, hanging drop vapor diffusion technique, 4°C, mixing of 7 mg/ml protein in 0.65 M ammonium sulfate and 0.1 M sodium acetate, pH 4.0, and with 3 mM adenyl-5'-yl imidodiphosphate, 5 mM magnesium chloride, and 5 mM pyruvic acid for the enzyme complex, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement