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| | <StructureSection load='2bzr' size='340' side='right'caption='[[2bzr]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2bzr' size='340' side='right'caption='[[2bzr]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bzr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bzr]] is a 6 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=2BZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZR FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Propionyl-CoA_carboxylase Propionyl-CoA carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.3 6.4.1.3] </span></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]] 2.2Å</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=2bzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzr OCA], [https://pdbe.org/2bzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzr RCSB], [https://www.ebi.ac.uk/pdbsum/2bzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzr ProSAT], [https://www.topsan.org/Proteins/XMTB/2bzr TOPSAN]</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=2bzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzr OCA], [https://pdbe.org/2bzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzr RCSB], [https://www.ebi.ac.uk/pdbsum/2bzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzr ProSAT], [https://www.topsan.org/Proteins/XMTB/2bzr TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ACCD5_MYCTU ACCD5_MYCTU] Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate (PubMed:16354663, PubMed:16385038, PubMed:28222482). When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA (PubMed:16354663, PubMed:16385038, PubMed:28222482). Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex (PubMed:28222482).<ref>PMID:16354663</ref> <ref>PMID:16385038</ref> <ref>PMID:28222482</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]]
| + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Propionyl-CoA carboxylase]]
| + | [[Category: Holton SJ]] |
| - | [[Category: Holton, S J]]
| + | |
| - | [[Category: Accase]]
| + | |
| - | [[Category: Fatty acid biosynthesis]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Mycobacterium tuberculosis]] | + | |
| - | [[Category: Mycobacterium tuberculosis structural proteomics project]] | + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xmtb]]
| + | |
| Structural highlights
Function
ACCD5_MYCTU Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate (PubMed:16354663, PubMed:16385038, PubMed:28222482). When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA (PubMed:16354663, PubMed:16385038, PubMed:28222482). Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex (PubMed:28222482).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mycobacterium tuberculosis contains multiple versions of the accA and accD genes that encode the alpha- and beta-subunits of at least three distinct multi-functional acyl-CoA carboxylase complexes. Because of its proposed involvement in pathogenic M. tuberculosis survival, the high-resolution crystal structure of the beta-subunit gene accD5 product has been determined and reveals a hexameric 356 kDa complex. Analysis of the active site properties of AccD5 and homology models of the other five M. tuberculosis AccD homologues reveals unexpected differences in their surface composition, providing a molecular rational key for a sorting mechanism governing correct acyl-CoA carboxylase holo complex assembly in M. tuberculosis.
Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis.,Holton SJ, King-Scott S, Nasser Eddine A, Kaufmann SH, Wilmanns M FEBS Lett. 2006 Dec 22;580(30):6898-902. Epub 2006 Nov 30. PMID:17157300[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oh TJ, Daniel J, Kim HJ, Sirakova TD, Kolattukudy PE. Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. J Biol Chem. 2006 Feb 17;281(7):3899-908. PMID:16354663 doi:10.1074/jbc.M511761200
- ↑ Gago G, Kurth D, Diacovich L, Tsai SC, Gramajo H. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J Bacteriol. 2006 Jan;188(2):477-86. PMID:16385038 doi:10.1128/JB.188.2.477-486.2006
- ↑ Bazet Lyonnet B, Diacovich L, Gago G, Spina L, Bardou F, Lemassu A, Quémard A, Gramajo H. Functional reconstitution of the Mycobacterium tuberculosis long-chain acyl-CoA carboxylase from multiple acyl-CoA subunits. FEBS J. 2017 Apr;284(7):1110-1125. PMID:28222482 doi:10.1111/febs.14046
- ↑ Holton SJ, King-Scott S, Nasser Eddine A, Kaufmann SH, Wilmanns M. Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett. 2006 Dec 22;580(30):6898-902. Epub 2006 Nov 30. PMID:17157300 doi:http://dx.doi.org/10.1016/j.febslet.2006.11.054
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