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| [[Image:1k92.gif|left|200px]]
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| {{Structure
| | ==Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase== |
| |PDB= 1k92 |SIZE=350|CAPTION= <scene name='initialview01'>1k92</scene>, resolution 1.60Å
| | <StructureSection load='1k92' size='340' side='right'caption='[[1k92]], [[Resolution|resolution]] 1.60Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
| | <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> |
| |ACTIVITY= <span class='plainlinks'>[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] </span>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| |GENE= ARGG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| | <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> |
| |DOMAIN=
| | <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> |
| |RELATEDENTRY=[[1k97|1K97]]
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k92 OCA], [http://www.ebi.ac.uk/pdbsum/1k92 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k92 RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/ASSY_ECOLI ASSY_ECOLI] |
| | | == Evolutionary Conservation == |
| '''Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase'''
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | | Check<jmol> |
| | | <jmolCheckbox> |
| ==Overview== | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/1k92_consurf.spt"</scriptWhenChecked> |
| 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.
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | | <text>to colour the structure by Evolutionary Conservation</text> |
| ==About this Structure== | | </jmolCheckbox> |
| 1K92 is a [[Single protein]] structure of 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=1K92 OCA].
| | </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> |
| ==Reference== | | __TOC__ |
| 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://www.ncbi.nlm.nih.gov/pubmed/11738042 11738042]
| | </StructureSection> |
| [[Category: Argininosuccinate synthase]]
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| [[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: n-type atp pyrophosphatase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:11 2008''
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