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3pgq

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==Crystal Structure of the Carboxyltransferase Domain of S. cerevisiae Acetyl CoA Carboxylase in Complex with Pinoxaden==
==Crystal Structure of the Carboxyltransferase Domain of S. cerevisiae Acetyl CoA Carboxylase in Complex with Pinoxaden==
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<StructureSection load='3pgq' size='340' side='right' caption='[[3pgq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='3pgq' size='340' side='right'caption='[[3pgq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pgq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PGQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pgq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGQ 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=GY3:8-(2-ETHENYL-6-ETHYL-4-METHYLPHENYL)TETRAHYDRO-7H-PYRAZOLO[1,2-D][1,4,5]OXADIAZEPINE-7,9(8H)-DIONE'>GY3</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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k8x|3k8x]], [[1od4|1od4]], [[1uyr|1uyr]], [[1uys|1uys]], [[1uyt|1uyt]], [[1uyv|1uyv]]</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=GY3:8-(2-ETHENYL-6-ETHYL-4-METHYLPHENYL)TETRAHYDRO-7H-PYRAZOLO[1,2-D][1,4,5]OXADIAZEPINE-7,9(8H)-DIONE'>GY3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAS3, ACC1, YNR016C, N3175 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3pgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgq OCA], [https://pdbe.org/3pgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pgq RCSB], [https://www.ebi.ac.uk/pdbsum/3pgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgq ProSAT]</span></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/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=3pgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgq OCA], [http://pdbe.org/3pgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pgq RCSB], [http://www.ebi.ac.uk/pdbsum/3pgq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACAC_YEAST ACAC_YEAST]] Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.<ref>PMID:6108218</ref> <ref>PMID:6103540</ref> <ref>PMID:8943372</ref> <ref>PMID:10757783</ref> <ref>PMID:12730220</ref>
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[https://www.uniprot.org/uniprot/ACAC_YEAST ACAC_YEAST] Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.<ref>PMID:6108218</ref> <ref>PMID:6103540</ref> <ref>PMID:8943372</ref> <ref>PMID:10757783</ref> <ref>PMID:12730220</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acetyl-CoA carboxylases (ACCs) are crucial metabolic enzymes and have been targeted for drug development against obesity, diabetes, and other diseases. The carboxyltransferase (CT) domain of this enzyme is the site of action for three different classes of herbicides, as represented by haloxyfop, tepraloxydim, and pinoxaden. Our earlier studies have demonstrated that haloxyfop and tepraloxydim bind in the CT active site at the interface of its dimer. However, the two compounds probe distinct regions of the dimer interface, sharing primarily only two common anchoring points of interaction with the enzyme. We report here the crystal structure of the CT domain of yeast ACC in complex with pinoxaden at 2.8-A resolution. Despite their chemical diversity, pinoxaden has a similar binding mode as tepraloxydim and requires a small conformational change in the dimer interface for binding. Crystal structures of the CT domain in complex with all three classes of herbicides confirm the importance of the two anchoring points for herbicide binding. The structures also provide a foundation for understanding the molecular basis of the herbicide resistance mutations and cross resistance among the herbicides, as well as for the design and development of new inhibitors against plant and human ACCs.
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Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden.,Yu LP, Kim YS, Tong L Proc Natl Acad Sci U S A. 2010 Dec 6. PMID:21135213<ref>PMID:21135213</ref>
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==See Also==
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*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
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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 3pgq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetyl-CoA carboxylase]]
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[[Category: Large Structures]]
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[[Category: Atcc 18824]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Kim, Y S]]
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[[Category: Kim YS]]
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[[Category: Tong, L]]
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[[Category: Tong L]]
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[[Category: Yu, L P.C]]
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[[Category: Yu LPC]]
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[[Category: Carboxyltransferase]]
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[[Category: Ligase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of the Carboxyltransferase Domain of S. cerevisiae Acetyl CoA Carboxylase in Complex with Pinoxaden

PDB ID 3pgq

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