5nil
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB section== | |
| + | <StructureSection load='5nil' size='340' side='right' caption='[[5nil]], [[Resolution|resolution]] 5.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5nil]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NIL FirstGlance]. <br> | ||
| + | </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=5nil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nil OCA], [http://pdbe.org/5nil PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nil RCSB], [http://www.ebi.ac.uk/pdbsum/5nil PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nil ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TOLC_ECOLI TOLC_ECOLI]] Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.<ref>PMID:6337123</ref> <ref>PMID:11274125</ref> <ref>PMID:15228545</ref> <ref>PMID:18955484</ref> <ref>PMID:23176499</ref> [[http://www.uniprot.org/uniprot/MACB_ECOLI MACB_ECOLI]] Part of the tripartite efflux system MacAB-TolC. 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. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid.<ref>PMID:11544226</ref> <ref>PMID:17214741</ref> <ref>PMID:18955484</ref> <ref>PMID:23974027</ref> [[http://www.uniprot.org/uniprot/MACA_ECOLI MACA_ECOLI]] Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP-bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system could also transport R-LPS or a similar glycolipid.<ref>PMID:11544226</ref> <ref>PMID:17214741</ref> <ref>PMID:18955484</ref> <ref>PMID:21696464</ref> <ref>PMID:23974027</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. | ||
| - | + | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump.,Fitzpatrick AWP, Llabres S, Neuberger A, Blaza JN, Bai XC, Okada U, Murakami S, van Veen HW, Zachariae U, Scheres SHW, Luisi BF, Du D Nat Microbiol. 2017 May 15;2:17070. doi: 10.1038/nmicrobiol.2017.70. PMID:28504659<ref>PMID:28504659</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5nil" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Bai, X C]] | ||
| + | [[Category: Blaza, J N]] | ||
[[Category: Du, D]] | [[Category: Du, D]] | ||
| - | [[Category: | + | [[Category: Fitzpatrick, A W.P]] |
| - | [[Category: | + | [[Category: Llabres, S]] |
| - | [[Category: | + | [[Category: Luisi, B F]] |
| - | [[Category: | + | [[Category: Murakami, S]] |
| - | + | ||
[[Category: Neuberger, A]] | [[Category: Neuberger, A]] | ||
| + | [[Category: Okada, U]] | ||
| + | [[Category: Scheres, S H.W]] | ||
| + | [[Category: Veen, H W.van]] | ||
| + | [[Category: Zachariae, U]] | ||
| + | [[Category: Abc transporter]] | ||
| + | [[Category: Drug efflux pump]] | ||
| + | [[Category: Macrolide transporter]] | ||
| + | [[Category: Multi-drug resistance]] | ||
| + | [[Category: Toxin transporter]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 13:40, 24 May 2017
Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB section
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Categories: Bai, X C | Blaza, J N | Du, D | Fitzpatrick, A W.P | Llabres, S | Luisi, B F | Murakami, S | Neuberger, A | Okada, U | Scheres, S H.W | Veen, H W.van | Zachariae, U | Abc transporter | Drug efflux pump | Macrolide transporter | Multi-drug resistance | Toxin transporter | Transport protein
