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homotrimer
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crystal structure
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x * 52000, SDS-PAGE
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x * 52000, SDS-PAGE
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x * 54100,, recombinant Histagged GlmU, SDS-PAGE
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x * 52965, recombinant His6-tagged enzyme, SDS-PAGE and mass spectrometry
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x * 52965, recombinant His6-tagged enzyme, SDS-PAGE and mass spectrometry
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heterotrimer
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trimer
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trimer
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2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration
trimer
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1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE
trimer
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2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration
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trimer
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1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE
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trimer
GlmU has a conserved two-domain architecture, one monomer per asymmetric unit, and a trimeric quaternary structure, modeling of acetyl-CoA bound to the C-terminal domain, overview
trimer
two-domain architecture of GlmU, one monomer per asymmetric unit, and a trimeric quaternary structure known for GlmU proteins
trimer
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
trimer
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the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
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trimer
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the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
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additional information
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
additional information
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the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
additional information
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the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
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additional information
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the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability. The distance between the GlcN-1-P AcTase and GlcNAc-1-P UTase catalytic centers is smaller in the ST0452 protein than the mesophilic bacterial GlmU
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additional information
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C324 does not form a disulphide bond with any other cysteine. This is consistent with the replacement of C307 by a serine in Y. pestis and the great distance between the three other cysteines (C296, C301 and C385) and C324
additional information
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C324 does not form a disulphide bond with any other cysteine. This is consistent with the replacement of C307 by a serine in Y. pestis and the great distance between the three other cysteines (C296, C301 and C385) and C324
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