4g2r: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g2r]] 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=4G2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G2R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g2r]] 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=4G2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G2R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H1L:(2R)-2-(4-{[3-CHLORO-5-(TRIFLUOROMETHYL)PYRIDIN-2-YL]OXY}PHENOXY)PROPANOIC+ACID'>H1L</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H1L:(2R)-2-(4-{[3-CHLORO-5-(TRIFLUOROMETHYL)PYRIDIN-2-YL]OXY}PHENOXY)PROPANOIC+ACID'>H1L</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=4g2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2r OCA], [https://pdbe.org/4g2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g2r RCSB], [https://www.ebi.ac.uk/pdbsum/4g2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g2r ProSAT]</span></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=4g2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2r OCA], [https://pdbe.org/4g2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g2r RCSB], [https://www.ebi.ac.uk/pdbsum/4g2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g2r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[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>  
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4g2r" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 15:38, 14 March 2024

Crystal Structure of the carboxyltransferase subunit of ACC (AccD6) in complex with inhibitor haloxyfop from Mycobacterium tuberculosis

4g2r, resolution 2.28Å

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