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1od2

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[[Image:1od2.gif|left|200px]]<br />
 
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<applet load="1od2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1od2, resolution 2.7&Aring;" />
 
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'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''<br />
 
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==Overview==
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==Acetyl-CoA Carboxylase Carboxyltransferase Domain==
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Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis, and oxidation of long-chain fatty acids. They are targets for therapeutics, against obesity and diabetes, and several herbicides function by, inhibiting their carboxyltransferase (CT) domain. We determined the, crystal structure of the free enzyme and the coenzyme A complex of yeast, CT at 2.7 angstrom resolution and found that it comprises two domains, both belonging to the crotonase/ClpP superfamily. The active site is at, the interface of a dimer. Mutagenesis and kinetic studies reveal the, functional roles of conserved residues here. The herbicides target the, active site of CT, providing a lead for inhibitor development against, human ACCs.
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<StructureSection load='1od2' size='340' side='right'caption='[[1od2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1od2]] is a 2 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=1OD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OD2 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]] 2.7&#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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1od2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1od2 OCA], [https://pdbe.org/1od2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1od2 RCSB], [https://www.ebi.ac.uk/pdbsum/1od2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1od2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== 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/od/1od2_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=1od2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1OD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ACO and ADE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OD2 OCA].
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*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase., Zhang H, Yang Z, Shen Y, Tong L, Science. 2003 Mar 28;299(5615):2064-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12663926 12663926]
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__TOC__
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[[Category: Acetyl-CoA carboxylase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Shen Y]]
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[[Category: Shen, Y.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: Yang Z]]
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[[Category: Yang, Z.]]
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[[Category: Zhang H]]
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[[Category: Zhang, H.]]
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[[Category: ACO]]
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[[Category: ADE]]
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[[Category: acc]]
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[[Category: acetyl-coa]]
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[[Category: acetyl-coa carboxylase]]
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[[Category: obesity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:50:12 2007''
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Current revision

Acetyl-CoA Carboxylase Carboxyltransferase Domain

PDB ID 1od2

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