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hexamer
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction
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x * 60000, SDS-PAGE
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x * 54500, calculated from amino acid sequence
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x * 58360, calculated from SDS-PAGE
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x * 58360, recombinant His-tagged enzyme, SDS-PAGE
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x * 49624, calculated from the deduced amino acid sequence of the His-tagged protein
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x * 55100, approximately, sequence calculation
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x * 55800, approximately, sequence calculation
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x * 52922, calculated
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x * 52922, calculated
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x * 54071, wild-type SPL29, sequence calculation, x * 54117, mutant spl29, sequence calculation
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x * 54071, wild-type SPL29, sequence calculation, x * 54117, mutant spl29, sequence calculation
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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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dimer
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2 * 33000, SDS-PAGE, gel filtration
dimer
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2 * 64000, SDS-PAGE, gel filtration
dimer
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1 * 64000 + 1 * 57000
monomer
1 * 58300, SDS-PAGE
monomer
1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration
trimer
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trimer
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3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer)
trimer
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction
trimer
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3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer)
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trimer
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x-ray crystallography
trimer
GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein
trimer
two-domain architecture of GlmU, one monomer per asymmetric unit, and a trimeric quaternary structure known for GlmU proteins
trimer
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x-ray crystallography
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trimer
crystal structure analysis
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
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
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
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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
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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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