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PDBsum entry 1gpm
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Transferase (glutamine amidotransferase)
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PDB id
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1gpm
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of gmp synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
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Authors
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J.J.Tesmer,
T.J.Klem,
M.L.Deras,
V.J.Davisson,
J.L.Smith.
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Ref.
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Nat Struct Biol, 1996,
3,
74-86.
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PubMed id
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Abstract
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The crystal structure of GMP synthetase serves as a prototype for two families
of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP
synthetase is found in related enzymes of the purine, pyrimidine, tryptophan,
arginine, histidine and folic acid biosynthetic pathways. This domain includes a
conserved Cys-His-Glu triad and is representative of a new family of enzymes
that use a catalytic triad for enzymatic hydrolysis. The structure and conserved
sequence fingerprint of the nucleotide-binding site in a second domain of GMP
synthetase are common to a family of ATP pyrophosphatases, including NAD
synthetase, asparagine synthetase and argininosuccinate synthetase.
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Secondary reference #1
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Title
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Preliminary X-Ray analysis of escherichia coli gmp synthetase: determination of anomalous scattering factors for a cysteinyl mercury derivative.
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Authors
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J.J.Tesmer,
T.L.Stemmler,
J.E.Penner-Hahn,
V.J.Davisson,
J.L.Smith.
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Ref.
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Proteins, 1994,
18,
394-403.
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PubMed id
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