1gpm

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{{STRUCTURE_1gpm| PDB=1gpm | SCENE= }}
{{STRUCTURE_1gpm| PDB=1gpm | SCENE= }}
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'''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''
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===ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 8548458 is the PubMed ID number.
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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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Revision as of 02:40, 1 July 2008

Image:1gpm.png

Template:STRUCTURE 1gpm

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

Template:ABSTRACT PUBMED 8548458

About this Structure

1GPM is a Single protein structure of sequence from Escherichia coli. 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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