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| | ==Structure of Aggregatibacter actinomycetemcomitans MacB bound to ATP (P21)== | | ==Structure of Aggregatibacter actinomycetemcomitans MacB bound to ATP (P21)== |
| - | <StructureSection load='5lj7' size='340' side='right' caption='[[5lj7]], [[Resolution|resolution]] 3.25Å' scene=''> | + | <StructureSection load='5lj7' size='340' side='right'caption='[[5lj7]], [[Resolution|resolution]] 3.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_acetinomycetum_comitans"_(sic)_(klinger_1912)_colebrook_1920 "bacterium acetinomycetum comitans" (sic) (klinger 1912) colebrook 1920]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LJ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aggregatibacter_actinomycetemcomitans Aggregatibacter actinomycetemcomitans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LJ7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.25Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">macB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=714 "Bacterium acetinomycetum comitans" (sic) (Klinger 1912) Colebrook 1920])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lj7 OCA], [http://pdbe.org/5lj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lj7 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=5lj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lj7 OCA], [https://pdbe.org/5lj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lj7 RCSB], [https://www.ebi.ac.uk/pdbsum/5lj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lj7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MACB_AGGAC MACB_AGGAC]] Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.<ref>PMID:19432486</ref> | + | [https://www.uniprot.org/uniprot/MACB_AGGAC MACB_AGGAC] Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.<ref>PMID:19432486</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Crow, A]] | + | [[Category: Aggregatibacter actinomycetemcomitans]] |
| - | [[Category: Abc transporter]] | + | [[Category: Large Structures]] |
| - | [[Category: Membrane protein]] | + | [[Category: Crow A]] |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
MACB_AGGAC Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[1]
Publication Abstract from PubMed
MacB is an ABC transporter that collaborates with the MacA adaptor protein and TolC exit duct to drive efflux of antibiotics and enterotoxin STII out of the bacterial cell. Here we present the structure of ATP-bound MacB and reveal precise molecular details of its mechanism. The MacB transmembrane domain lacks a central cavity through which substrates could be passed, but instead conveys conformational changes from one side of the membrane to the other, a process we term mechanotransmission. Comparison of ATP-bound and nucleotide-free states reveals how reversible dimerization of the nucleotide binding domains drives opening and closing of the MacB periplasmic domains via concerted movements of the second transmembrane segment and major coupling helix. We propose that the assembled tripartite pump acts as a molecular bellows to propel substrates through the TolC exit duct, driven by MacB mechanotransmission. Homologs of MacB that do not form tripartite pumps, but share structural features underpinning mechanotransmission, include the LolCDE lipoprotein trafficking complex and FtsEX cell division signaling protein. The MacB architecture serves as the blueprint for understanding the structure and mechanism of an entire ABC transporter superfamily and the many diverse functions it supports.
Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily.,Crow A, Greene NP, Kaplan E, Koronakis V Proc Natl Acad Sci U S A. 2017 Nov 6. pii: 201712153. doi:, 10.1073/pnas.1712153114. PMID:29109272[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Y, Sim SH, Nam KH, Jin XL, Kim HM, Hwang KY, Lee K, Ha NC. Crystal Structure of the Periplasmic Region of MacB, a Noncanonic ABC Transporter (,). Biochemistry. 2009 May 21. PMID:19432486 doi:10.1021/bi900415t
- ↑ Crow A, Greene NP, Kaplan E, Koronakis V. Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily. Proc Natl Acad Sci U S A. 2017 Nov 6. pii: 201712153. doi:, 10.1073/pnas.1712153114. PMID:29109272 doi:http://dx.doi.org/10.1073/pnas.1712153114
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