1gpm: Difference between revisions
New page: left|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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[[Image:1gpm.gif|left|200px]]<br /><applet load="1gpm" size=" | [[Image:1gpm.gif|left|200px]]<br /><applet load="1gpm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gpm, resolution 2.2Å" /> | caption="1gpm, resolution 2.2Å" /> | ||
'''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''<br /> | '''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of GMP synthetase serves as a prototype for two | 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== | ==About this Structure== | ||
1GPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, MG, POP, AMP and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] Full crystallographic information is available from [http:// | 1GPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=POP:'>POP</scene>, <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: GMP synthase (glutamine-hydrolyzing)]] | [[Category: GMP synthase (glutamine-hydrolyzing)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tesmer, J | [[Category: Tesmer, J J.G.]] | ||
[[Category: AMP]] | [[Category: AMP]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
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[[Category: n-type atp pyrophosphatase]] | [[Category: n-type atp pyrophosphatase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:39 2008'' | ||
Revision as of 13:52, 21 February 2008
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ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE
OverviewOverview
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 StructureAbout this Structure
1GPM is a Single protein structure of sequence from Escherichia coli with , , , and as ligands. Active as GMP synthase (glutamine-hydrolyzing), with EC number 6.3.5.2 Full crystallographic information is available from OCA.
ReferenceReference
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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