1gpm: Difference between revisions

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{{STRUCTURE_1gpm|  PDB=1gpm  |  SCENE=  }}  
{{STRUCTURE_1gpm|  PDB=1gpm  |  SCENE=  }}  


'''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''
===ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE===




==Overview==
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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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==About this Structure==
==About this Structure==
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[[Category: Class i glutamine amidotransferase]]
[[Category: Class i glutamine amidotransferase]]
[[Category: N-type atp pyrophosphatase]]
[[Category: N-type atp pyrophosphatase]]
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