5mlk

From Proteopedia

(Difference between revisions)

Current revision

Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)

Structural highlights

5mlk is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.939Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

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.

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^[5]

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
↑ Daniel J, Oh TJ, Lee CM, Kolattukudy PE. AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis. J Bacteriol. 2007 Feb;189(3):911-7. doi: 10.1128/JB.01019-06. Epub 2006 Nov 17. PMID:17114269 doi:http://dx.doi.org/10.1128/JB.01019-06
↑ 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
↑ Bennett M, Hogbom M. Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis. FEBS Open Bio. 2017 Apr 4;7(5):620-626. doi: 10.1002/2211-5463.12212. eCollection, 2017 May. PMID:28469974 doi:http://dx.doi.org/10.1002/2211-5463.12212

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5mlk"

Categories: Large Structures | Mycobacterium tuberculosis H37Rv | Bennett MD | Hogbom M

@@ Line 3: / Line 3: @@
 <StructureSection load='5mlk' size='340' side='right'caption='[[5mlk]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5mlk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5MLK FirstGlance]. <br>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">accA3, Rv3285, LH57_17955 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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]] 1.939&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mlk OCA], [http://pdbe.org/5mlk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mlk RCSB], [http://www.ebi.ac.uk/pdbsum/5mlk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mlk 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=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>
+== 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 ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Myctu]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Bennett, M D]]
+[[Category: Bennett MD]]
-[[Category: Hogbom, M]]
+[[Category: Hogbom M]]
-[[Category: Biotin dependant carboxylase]]
-[[Category: Grasp]]
-[[Category: Ligase]]

5mlk

From Proteopedia

Current revision

Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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