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• W1977681633 abstract "The amino acid sequence of glycolate oxidase from spinach has been fitted to an electron density map of 2.0 Å nominal resolution and the structure has been refined using the restrained parameter least-squares refinement of Hendrickson and Konnert. A final crystallographic R-factor of 18.9% was obtained for 32,888 independent reflections from 5.5 to 2 Å resolution. The geometry of the model, consisting of 350 amino acid residues, the cofactor flavin mononucleotide and 298 solvent molecules, is close to ideal with root-means-quare deviations of 0.015 Å in bond lengths and 2.6 ° in bond angles. The expected trimodal distribution with preference for staggered conformation is obtained for the side-chain χ1-angles. The core of the subunit is built up from the eight β-strands in the βα-barrel. This core consists of two hydrophobic layers. One in the center is made up of residues pointing in from the β-strands towards the barrel axis and the second, consisting of two segments of residues, pointing out from the β-strands towards the eight α-helices of the barrel and pointing from the helices towards the strands. The hydrogen bond pattern for the β-strands in the βα-barrel is described. There are a number of residues with 310-helix conformation, in particular there is one left-handed helix. The ordered solvent molecules are organized mainly in clusters. The average isotropic temperature factor is quite high, 27.1 Å2, perhaps a reflection of the high solvent content in the crystal. The octameric glycolate oxidase molecule, which has 422 symmetry, makes strong interactions around the 4-fold axis forming a tight tetramer, but only weak interactions between the two tetramers forming the octamer." @default.
• W1977681633 created "2016-06-24" @default.
• W1977681633 creator A5053178273 @default.
• W1977681633 date "1989-09-01" @default.
• W1977681633 modified "2023-10-16" @default.
• W1977681633 title "Refined structure of spinach glycolate oxidase at 2 Å resolution" @default.
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• W1977681633 doi "https://doi.org/10.1016/0022-2836(89)90178-2" @default.
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