1od2

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{{Seed}}
 
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[[Image:1od2.png|left|200px]]
 
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==Acetyl-CoA Carboxylase Carboxyltransferase Domain==
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The line below this paragraph, containing "STRUCTURE_1od2", creates the "Structure Box" on the page.
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<StructureSection load='1od2' size='340' side='right'caption='[[1od2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1od2| PDB=1od2 | SCENE= }}
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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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN===
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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:12663926<ref>PMID:12663926</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 1od2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12663926}}, adds the Publication Abstract to the page
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*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12663926 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12663926}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1OD2 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12663926 12663926]
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[[Category: Acetyl-CoA carboxylase]]
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[[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: 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://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:55:30 2008''
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Current revision

Acetyl-CoA Carboxylase Carboxyltransferase Domain

PDB ID 1od2

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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