Structures were solved by molecular replacement using MolRep version Note that the protomer colored with blue helices and green strands is in the same orientation as that shown in Fig. Eur J Biochem. Reuss J. Nat Struct Biol. Our data suggest that the presence of oxygen atoms in the outer molecular shell is an important factor for the fast translocation ability of lipophilic anions.
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Reuss J. This phosphate is in hydrogen bonding distance with the two backbone amides of Asp, Thr and Gly as well as the side chain of Thr Sukhorukov 3 Email author 1.
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Phosphoribosylpyrophosphate and purine metabolism in cultured fibroblasts. DecemberCite as. Synthesis and metabolic fate of purine nucleotides in cultured fibroblasts from normal subjects and from purine overproducing mutants.
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Vagin A, Teplyakov A. Among other parameters discussed above i.
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Structural and mechanistic studies on Klebsiella pneumoniae 2-Oxohydroxycarboxyureidoimidazoline decarboxylase. Personalised recommendations. Protein expression and purification The E. After the refinement had converged, water molecules were added using Coot. Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase.
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EcKPRS forms a propeller-shaped hexamer with 32 point symmetry a. At each field frequency, the rotation speed of an individual cell located near the center of the chamber was determined using a stopwatch. Benz R, Nonner W Structure of the axolemma of frog myelinated nerve—relaxation experiments with a lipophilic probe ion.
ROT spectra were monitored by decreasing the field frequency in steps four frequency points per decade. Otwinowski Z, Minor W. |
J Membrane Biol () Weijie Zhou; Andrew Tsai; Devon A. Dattmore; Devin P. Stives; Iva Chitrakar; Alexis M. D'alessandro; Shiv Patil; Katherine A.
90, 90, 90 . Metabolism of nucleotides, nucleosides and nucleobases in micro-organisms.
Skip to main content Skip to sections. The R5P binding site is known to be made up of residues from the C-terminal region of a single chain. Dysfunction of this protein in humans can lead to severe neurodevelopmental disability. This finding can be explained by the assumption that the adsorption plane of large organic anions moved slightly toward the center of the membrane as the concentration of adsorbed anions increases.
EcKPRS forms a propeller-shaped hexamer with 32 point symmetry a. Both domains have a type I phosphoribosyltransferase fold. Open image in new window.
While the density is not sufficient to accommodate the full nucleotide structure, it is possible that this density results from partial occupancy or some level of inherent flexibility of the nucleotide in the absence of the R5P co-substrate. The C-terminal domain of each protomer dimerizes with one other C-terminal domain to form the blades of the propeller, while the N-terminal domains form the inner core of the structure Fig.
PRPP synthetase is an important enzyme that produces a key metabolic intermediate necessary for the biosynthesis of purine and pyrimidine nucleotides.
Among other parameters discussed above i.