1za2

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[[Image:1za2.gif|left|200px]]
 
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==Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution==
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The line below this paragraph, containing "STRUCTURE_1za2", creates the "Structure Box" on the page.
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<StructureSection load='1za2' size='340' side='right'caption='[[1za2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1za2]] is a 4 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=1ZA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZA2 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]] 2.5&#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=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1za2| PDB=1za2 | SCENE= }}
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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=1za2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1za2 OCA], [https://pdbe.org/1za2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1za2 RCSB], [https://www.ebi.ac.uk/pdbsum/1za2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1za2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
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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/za/1za2_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=1za2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity.
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'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution'''
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Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.,Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:15951418<ref>PMID:15951418</ref>
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==Overview==
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X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ZA2 is a [[Protein complex]] structure of sequences 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=1ZA2 OCA].
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</div>
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<div class="pdbe-citations 1za2" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase., Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER, Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15951418 15951418]
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*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
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[[Category: Aspartate carbamoyltransferase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Cardia, J P.]]
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[[Category: Cardia JP]]
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[[Category: Kantrowitz, E R.]]
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[[Category: Kantrowitz ER]]
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[[Category: Stieglitz, K A.]]
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[[Category: Stieglitz KA]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: Cooperativity]]
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[[Category: Ordered substrate binding]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:22:27 2008''
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Current revision

Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution

PDB ID 1za2

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