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 2.2&Aring;" /> '''ESCHERICHIA COLI GMP ...)
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[[Image:1gpm.gif|left|200px]]<br /><applet load="1gpm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gpm, resolution 2.2&Aring;" />
 
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'''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''<br />
 
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==Overview==
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==ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE==
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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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<StructureSection load='1gpm' size='340' side='right'caption='[[1gpm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gpm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpm OCA], [https://pdbe.org/1gpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpm RCSB], [https://www.ebi.ac.uk/pdbsum/1gpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUAA_ECOLI GUAA_ECOLI] Catalyzes the synthesis of GMP from XMP.[HAMAP-Rule:MF_00344]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gpm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gpm ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPM OCA].
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*[[GMP synthase|GMP synthase]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8548458 8548458]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: GMP synthase (glutamine-hydrolyzing)]]
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[[Category: Tesmer JJG]]
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[[Category: Single protein]]
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[[Category: Tesmer, J.J.G.]]
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[[Category: AMP]]
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[[Category: CIT]]
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[[Category: MG]]
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[[Category: PO4]]
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[[Category: POP]]
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[[Category: class i glutamine amidotransferase]]
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[[Category: n-type atp pyrophosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:13:24 2007''
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Current revision

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

PDB ID 1gpm

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