1za2

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{{STRUCTURE_1za2| PDB=1za2 | SCENE= }}
 
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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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{{ABSTRACT_PUBMED_15951418}}
 
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==Function==
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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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[[http://www.uniprot.org/uniprot/PYRI_ECOLI PYRI_ECOLI]] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002]
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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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<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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<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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==About this Structure==
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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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[[1za2]] is a 4 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=1ZA2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:015951418</ref><references group="xtra"/><references/>
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</div>
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[[Category: Aspartate carbamoyltransferase]]
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<div class="pdbe-citations 1za2" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
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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: Cardia, J P.]]
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[[Category: Large Structures]]
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[[Category: Kantrowitz, E R.]]
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[[Category: Cardia JP]]
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[[Category: Stieglitz, K A.]]
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[[Category: Kantrowitz ER]]
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[[Category: Wang, J.]]
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[[Category: Stieglitz KA]]
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[[Category: Cooperativity]]
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[[Category: Wang J]]
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[[Category: Ordered substrate binding]]
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[[Category: Transferase]]
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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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