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- W1991728222 abstract "The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 Å resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 Å resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 Å in bond length and 3.5 ° in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 Å. The refinement confirmed the heterodox, non-parallel character of the 8-fold βα-barrel domain with ββαα(βα)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 Å from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds." @default.
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- W1991728222 date "1990-01-01" @default.
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- W1991728222 title "Refined structure of yeast apo-enolase at 2.25 Å resolution" @default.
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- W1991728222 doi "https://doi.org/10.1016/0022-2836(90)90023-f" @default.
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