4f04

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==A Second Allosteric site in E. coli Aspartate Transcarbamoylase: R-state ATCase with UTP bound==
==A Second Allosteric site in E. coli Aspartate Transcarbamoylase: R-state ATCase with UTP bound==
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<StructureSection load='4f04' size='340' side='right' caption='[[4f04]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4f04' size='340' side='right'caption='[[4f04]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f04]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F04 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f04]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F04 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4245, JW4204, pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4244, JW4203, pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></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=4f04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f04 OCA], [https://pdbe.org/4f04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f04 RCSB], [https://www.ebi.ac.uk/pdbsum/4f04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f04 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f04 OCA], [http://pdbe.org/4f04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f04 RCSB], [http://www.ebi.ac.uk/pdbsum/4f04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f04 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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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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[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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E. coli aspartate transcarbamoylase is feedback inhibited by CTP and by UTP in the presence of CTP. Here, we show by X-ray crystallography that UTP binds to a unique site on each regulatory chain of the enzyme that is near to but not overlapping with the known CTP site. These results bring into question all of the previously proposed mechanisms of allosteric regulation in aspartate transcarbamoylase.
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A Second Allosteric Site in E. coli Aspartate Transcarbamoylase.,Peterson AW, Cockrell GM, Kantrowitz ER Biochemistry. 2012 Jun 5. PMID:22667327<ref>PMID:22667327</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4f04" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Aspartate carbamoyltransferase|Aspartate carbamoyltransferase]]
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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__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspartate carbamoyltransferase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ecoli]]
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[[Category: Large Structures]]
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[[Category: Cockrell, G M]]
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[[Category: Cockrell GM]]
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[[Category: Kantrowitz, E R]]
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[[Category: Kantrowitz ER]]
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[[Category: Peterson, A W]]
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[[Category: Peterson AW]]
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[[Category: Allosteric regulation]]
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[[Category: Atcase]]
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[[Category: Transferase]]
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Current revision

A Second Allosteric site in E. coli Aspartate Transcarbamoylase: R-state ATCase with UTP bound

PDB ID 4f04

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