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4fb8

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==Crystal Structure of apo Acyl-CoA Carboxylase==
==Crystal Structure of apo Acyl-CoA Carboxylase==
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<StructureSection load='4fb8' size='340' side='right' caption='[[4fb8]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4fb8' size='340' side='right'caption='[[4fb8]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fb8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FB8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FB8 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g2r|4g2r]]</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]] 3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">accD6, MT2307, MTCY427.28, Rv2247 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4fb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fb8 OCA], [https://pdbe.org/4fb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fb8 RCSB], [https://www.ebi.ac.uk/pdbsum/4fb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fb8 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Propionyl-CoA_carboxylase Propionyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.3 6.4.1.3] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fb8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fb8 RCSB], [http://www.ebi.ac.uk/pdbsum/4fb8 PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/ACCD6_MYCTU ACCD6_MYCTU] Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate (PubMed:17114269). When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for acetyl-CoA (PubMed:17114269).<ref>PMID:17114269</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In Mycobacterium tuberculosis (Mtb) the carboxylation of acetyl-CoA to produce malonyl-CoA, a building block in long chain fatty acid biosynthesis, is catalyzed by two enzymes working sequentially: a biotin carboxylase (AccA), and a carboxyltransferase (AccD). While the exact roles of the three different biotin carboxylases (AccA1-3) and the six carboxyltransferases (AccD1-6) in Mtb are still not clear, AccD6 in complex with AccA3 can synthesize malonyl-CoA from acetyl-CoA. A series of ten herbicides that target plant acetyl-CoA carboxylases (ACC) were tested for inhibition of AccD6 and for whole-cell activity against Mtb. From the tested herbicides, haloxyfop, an arylophenoxypropionate, showed in vitro inhibition of Mtb AccD6, with an IC50 = 21.4 +/- 1 muM. Here, we report the crystal structures of Mtb AccD6 in the apo form (3.0 A) and in complex with haloxyfop-R (2.3 A). The structure of Mtb AccD6 in complex with haloxyfop-R shows two molecules of the inhibitor bound on each AccD6 subunit. These results represent the potential for developing novel therapeutics for tuberculosis based on herbicides with low human toxicity.
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Structure, Activity, and Inhibition of the Carboxyltransferase beta-subunit of Acetyl-CoA Carboxylase (AccD6) from Mycobacterium tuberculosis.,Reddy MC, Breda A, Bruning JB, Sherekar M, Valluru S, Thurman C, Ehrenfeld H, Sacchettini JC Antimicrob Agents Chemother. 2014 Aug 4. pii: AAC.02574-13. PMID:25092705<ref>PMID:25092705</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Propionyl-CoA carboxylase]]
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[[Category: Large Structures]]
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[[Category: Bruning, J B.]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Ehrenfeld, H.]]
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[[Category: Bruning JB]]
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[[Category: Reddy, M C.M.]]
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[[Category: Ehrenfeld H]]
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[[Category: Sacchettini, J C.]]
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[[Category: Reddy MCM]]
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[[Category: Sherekar, M.]]
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[[Category: Sacchettini JC]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Sherekar M]]
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[[Category: Valluru, S.]]
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[[Category: Valluru S]]
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[[Category: Acyl-coa carboxylase]]
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[[Category: Crotonase fold]]
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[[Category: Ligase]]
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[[Category: Structural genomic]]
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[[Category: Tb structural genomics consortium]]
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[[Category: Tbsgc]]
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Current revision

Crystal Structure of apo Acyl-CoA Carboxylase

PDB ID 4fb8

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