1gpm
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(New page: 200px<br /><applet load="1gpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gpm, resolution 2.2Å" /> '''ESCHERICHIA COLI GMP ...)
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Revision as of 14:06, 20 November 2007
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ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE
Overview
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.
About this Structure
1GPM is a Single protein structure of sequence from Escherichia coli with PO4, MG, POP, AMP and CIT as ligands. Active as GMP synthase (glutamine-hydrolyzing), with EC number 6.3.5.2 Full crystallographic information is available from OCA.
Reference
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families., Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL, Nat Struct Biol. 1996 Jan;3(1):74-86. PMID:8548458
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