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New page: left|200px<br /><applet load="1k92" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k92, resolution 1.60Å" /> '''Crystal Structure of...
 
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[[Image:1k92.gif|left|200px]]<br /><applet load="1k92" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1k92, resolution 1.60&Aring;" />
'''Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase'''<br />


==Overview==
==Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase==
BACKGROUND: Argininosuccinate synthetase (AS) is the rate-limiting enzyme, of both the urea and arginine-citrulline cycles. In mammals, deficiency of, AS leads to citrullinemia, a debilitating and often fatal autosomal, recessive urea cycle disorder, whereas its overexpression for sustained, nitric oxide production via the arginine-citrulline cycle leads to the, potentially fatal hypotension associated with septic and cytokine-induced, circulatory shock. RESULTS: The crystal structure of E. coli AS (EAS) has, been determined by the use of selenomethionine incorporation and MAD, phasing. The structure has been refined at 1.6 A resolution in the absence, of its substrates and at 2.0 A in the presence of aspartate and citrulline, (EAS*CIT+ASP). Each monomer of this tetrameric protein has two structural, domains: a nucleotide binding domain similar to that of the "N-type" ATP, pyrophosphatase class of enzymes, and a novel catalytic/multimerization, domain. The EAS*CIT+ASP structure clearly describes the binding of, citrulline at the cleft between the two domains and of aspartate to a loop, of the nucleotide binding domain, whereas homology modeling with the, N-type ATP pyrophosphatases has provided the location of ATP binding., CONCLUSIONS: The first three-dimensional structures of AS are reported., The fold of the nucleotide binding domain confirms AS as the fourth, structurally defined member of the N-type ATP pyrophosphatases. The, structures identify catalytically important residues and suggest the, requirement for a conformational change during the catalytic cycle., Sequence similarity between the bacterial and human enzymes has been used, for providing insight into the structural and functional effects of, observed clinical mutations.
<StructureSection load='1k92' size='340' side='right'caption='[[1k92]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1k92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K92 FirstGlance]. <br>
1K92 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Argininosuccinate_synthase Argininosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.5 6.3.4.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K92 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k92 OCA], [https://pdbe.org/1k92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k92 RCSB], [https://www.ebi.ac.uk/pdbsum/1k92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k92 ProSAT]</span></td></tr>
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis., Lemke CT, Howell PL, Structure. 2001 Dec;9(12):1153-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11738042 11738042]
</table>
[[Category: Argininosuccinate synthase]]
== Function ==
[https://www.uniprot.org/uniprot/ASSY_ECOLI ASSY_ECOLI]
== 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/k9/1k92_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=1k92 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Howell, P.L.]]
[[Category: Howell PL]]
[[Category: Lemke, C.T.]]
[[Category: Lemke CT]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: n-type atp pyrophosphatase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:58:06 2007''

Latest revision as of 07:45, 7 February 2024

Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase

1k92, resolution 1.60Å

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