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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="450" color="white" frame="true" align="right" spinBox="true"
caption="1gpm, resolution 2.2&Aring;" />
'''ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE'''<br />


==Overview==
==ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE==
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.
<StructureSection load='1gpm' size='340' side='right'caption='[[1gpm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUAA_ECOLI GUAA_ECOLI] Catalyzes the synthesis of GMP from XMP.[HAMAP-Rule:MF_00344]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gpm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[GMP synthase|GMP synthase]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: GMP synthase (glutamine-hydrolyzing)]]
[[Category: Tesmer JJG]]
[[Category: Single protein]]
[[Category: Tesmer, J.J.G.]]
[[Category: AMP]]
[[Category: CIT]]
[[Category: MG]]
[[Category: PO4]]
[[Category: POP]]
[[Category: class i glutamine amidotransferase]]
[[Category: n-type atp pyrophosphatase]]
 
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