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==The crystal structure of carboxyltransferase from Staphylococcus Aureus bound to the antimicrobial agent moiramide B.==
<StructureSection load='5kdr' size='340' side='right'caption='[[5kdr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kdr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_RF122 Staphylococcus aureus RF122] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_USA300 Staphylococcus aureus subsp. aureus USA300]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KDR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YT5:MOIRAMIDE+B'>YT5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5kdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kdr OCA], [https://pdbe.org/5kdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kdr RCSB], [https://www.ebi.ac.uk/pdbsum/5kdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kdr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACCA_STAA8 ACCA_STAA8] Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.[HAMAP-Rule:MF_00823]
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== Publication Abstract from PubMed ==
The dramatic increase in antibiotic-resistant bacteria has necessitated a search for new antibacterial agents against novel targets. Moiramide B is a natural product, broad-spectrum antibiotic that inhibits the carboxyltransferase component of acetyl-CoA carboxylase, which catalyzes the first committed step in fatty acid synthesis. Herein, we report the 2.6 A resolution crystal structure of moiramide B bound to carboxyltransferase. An unanticipated, but significant finding was that moiramide B bound as the enol/enolate. Crystallographic studies demonstrate that the (4S)-methyl succinimide moiety interacts with the oxyanion holes of the enzyme, supporting the notion that an anionic enolate is the active form of the antibacterial agent. Structure-activity studies demonstrate that the unsaturated fatty acid tail of moiramide B is only needed for entry into the bacterial cell. These results will enable the design of new antibacterial agents against the bacterial form of carboxyltransferase.

The Crystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide B.,Silvers MA, Pakhomova S, Neau DB, Silvers WC, Anzalone N, Taylor CM, Waldrop GL Biochemistry. 2016 Jul 29. PMID:27471863<ref>PMID:27471863</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5kdr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus RF122]]
[[Category: Staphylococcus aureus subsp. aureus USA300]]
[[Category: Anzalone N]]
[[Category: Neau D]]
[[Category: Pakhomova S]]
[[Category: Silvers MA]]
[[Category: Silvers WC]]
[[Category: Taylor CM]]
[[Category: Waldrop GL]]