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- W2004201533 abstract "The recombinant synthase domain of the bifunctional enzyme N-(5″-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli has been crystallized, and the structure has been solved at 4 Å resolution. Two closely related crystal forms grown from ammonium sulphate diffract to 2 Å resolution. One form (space group R32, a = 163 Å, α = 29.5°) contains the unliganded synthase domain; the second crystal form (space group P6322, a = 144 Å, c = 158 Å) is co-crystallized with the substrate analogue N-(5′-phosphoribit-1-yl)anthranilate. The structure of the synthase–inhibitor complex has been solved by the molecular replacement method. This achievement represents the first successful use of a (βα)g-barrel monomer as a trial model. The recombinant synthase domain associates as a trimer in the crystal, the molecules being related by a pseudo-crystallographic triad. The interface contacts between the three domains are mediated by those residues that are also involved in the domain interface of the bifunctional enzyme. This system provides a model for an interface which is used in both intermolecular and intramolecular domain contacts." @default.
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- W2004201533 date "1990-01-01" @default.
- W2004201533 modified "2023-10-14" @default.
- W2004201533 title "Crystallization and structure solution at 4 Å resolution of the recombinant synthase domain of <i>N</i>(5′-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from <i>Escherichia coli</i> complexed to a substrate analogue" @default.
- W2004201533 doi "https://doi.org/10.1093/protein/3.3.173" @default.
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