5mlk
From Proteopedia
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==Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)== | ==Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)== | ||
| - | <StructureSection load='5mlk' size='340' side='right' caption='[[5mlk]], [[Resolution|resolution]] 1.94Å' scene=''> | + | <StructureSection load='5mlk' size='340' side='right'caption='[[5mlk]], [[Resolution|resolution]] 1.94Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5mlk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MLK OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5mlk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MLK FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.939Å</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=5mlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mlk OCA], [https://pdbe.org/5mlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mlk RCSB], [https://www.ebi.ac.uk/pdbsum/5mlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mlk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACCA3_MYCTU ACCA3_MYCTU] Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, resulting in the formation of carboxyl biotin (PubMed:16354663, PubMed:16385038, PubMed:17114269). When associated with the beta5 subunit AccD5, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA (PubMed:16354663, PubMed:16385038). When associated with the beta6 subunit AccD6, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for acetyl-CoA (PubMed:17114269). When associated with the beta4 subunit AccD4, the beta5 subunit AccD5 and the epsilon subunit AccE5, forms the LCC complex, which is involved in the carboxylation of long chain acyl-CoA (PubMed:16354663, PubMed:28222482). The LCC complex can use C16-C24 substrates, the highest specific activity is obtained with carboxy-C20-CoA (PubMed:28222482).<ref>PMID:16354663</ref> <ref>PMID:16385038</ref> <ref>PMID:17114269</ref> <ref>PMID:28222482</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in Mycobacterium tuberculosis (MTb). The structure, sequence comparisons, and modeling of ligand-bound states reveal that the ATP cosubstrate-binding site shows distinct differences compared to other bacterial and eukaryotic biotin carboxylases, including all human homologs. This suggests the possibility to design MTb AccA3 subtype-specific inhibitors. DATABASE: Coordinates and structure factors have been deposited in the Protein Data Bank with the accession number 5MLK. | ||
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| + | Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis.,Bennett M, Hogbom M FEBS Open Bio. 2017 Apr 4;7(5):620-626. doi: 10.1002/2211-5463.12212. eCollection, 2017 May. PMID:28469974<ref>PMID:28469974</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5mlk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: | + | [[Category: Bennett MD]] |
| - | [[Category: | + | [[Category: Hogbom M]] |
| - | + | ||
Current revision
Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)
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