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[[Image:1k97.png|left|200px]]


{{STRUCTURE_1k97| PDB=1k97 | SCENE= }}
==Crystal Structure of E. coli Argininosuccinate Synthetase in complex with Aspartate and Citrulline==
<StructureSection load='1k97' size='340' side='right'caption='[[1k97]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k97]] 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=1K97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K97 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CIR:CITRULLINE'>CIR</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=1k97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k97 OCA], [https://pdbe.org/1k97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k97 RCSB], [https://www.ebi.ac.uk/pdbsum/1k97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k97 ProSAT]</span></td></tr>
</table>
== 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/k9/1k97_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=1k97 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Crystal Structure of E. coli Argininosuccinate Synthetase in complex with Aspartate and Citrulline===
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:11738042<ref>PMID:11738042</ref>


{{ABSTRACT_PUBMED_11738042}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1k97" style="background-color:#fffaf0;"></div>
[[1k97]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K97 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:011738042</ref><references group="xtra"/>
</StructureSection>
[[Category: Argininosuccinate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Howell, P L.]]
[[Category: Large Structures]]
[[Category: Lemke, C T.]]
[[Category: Howell PL]]
[[Category: Ligase]]
[[Category: Lemke CT]]
[[Category: N-type atp pyrophosphatase]]
Retrieved from "https://proteopedia.org/1k97"