3r7f

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<StructureSection load='3r7f' size='340' side='right'caption='[[3r7f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3r7f' size='340' side='right'caption='[[3r7f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r7f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R7F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r7f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R7F FirstGlance]. <br>
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</td></tr><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=PO4:PHOSPHATE+ION'>PO4</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]] 2.101&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r7d|3r7d]], [[3r7l|3r7l]]</div></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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrB, BSU15490 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [https://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=3r7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r7f OCA], [https://pdbe.org/3r7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r7f RCSB], [https://www.ebi.ac.uk/pdbsum/3r7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r7f ProSAT]</span></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=3r7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r7f OCA], [https://pdbe.org/3r7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r7f RCSB], [https://www.ebi.ac.uk/pdbsum/3r7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r7f ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PYRB_BACSU PYRB_BACSU]
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Here, we report high-resolution X-ray structures of Bacillus subtilis aspartate transcarbamoylase (ATCase), an enzyme that catalyzes one of the first reactions in pyrimidine nucleotide biosynthesis. Structures of the enzyme have been determined in the absence of ligands, in the presence of the substrate carbamoyl phosphate, and in the presence of the bisubstrate/transition state analog N-phosphonacetyl-l-aspartate. Combining the structural data with in silico docking and electrostatic calculations, we have been able to visualize each step in the catalytic cycle of ATCase, from the ordered binding of the substrates, to the formation and decomposition of the tetrahedral intermediate, to the ordered release of the products from the active site. Analysis of the conformational changes associated with these steps provides a rationale for the lack of cooperativity in trimeric ATCases that do not possess regulatory subunits.
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Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilis.,Harris KM, Cockrell GM, Puleo DE, Kantrowitz ER J Mol Biol. 2011 May 31. PMID:21663747<ref>PMID:21663747</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 3r7f" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
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[[Category: Aspartate carbamoyltransferase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cockrell, G M]]
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[[Category: Cockrell GM]]
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[[Category: Harris, K M]]
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[[Category: Harris KM]]
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[[Category: Kantrowitz, E R]]
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[[Category: Kantrowitz ER]]
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[[Category: Puleo, D E]]
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[[Category: Puleo DE]]
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[[Category: Aspartate transcarbamoylase]]
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[[Category: Carbamoyl phosphate]]
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[[Category: Catalytic cycle]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of CP-bound Aspartate Transcarbamoylase from Bacillus subtilis

PDB ID 3r7f

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