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- PDB-5nik: Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump -
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Open data
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Basic information
Entry | Database: PDB / ID: 5nik | |||||||||
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Title | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump | |||||||||
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![]() | TRANSPORT PROTEIN / ABC transporter / drug efflux pump / multi-drug resistance / macrolide transporter / toxin transporter | |||||||||
Function / homology | ![]() MacAB-TolC complex / enterobactin transport / bile acid transmembrane transporter activity / xenobiotic detoxification by transmembrane export across the cell outer membrane / efflux pump complex / periplasmic side of plasma membrane / xenobiotic detoxification by transmembrane export across the plasma membrane / bile acid and bile salt transport / ABC-type xenobiotic transporter activity / Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate ...MacAB-TolC complex / enterobactin transport / bile acid transmembrane transporter activity / xenobiotic detoxification by transmembrane export across the cell outer membrane / efflux pump complex / periplasmic side of plasma membrane / xenobiotic detoxification by transmembrane export across the plasma membrane / bile acid and bile salt transport / ABC-type xenobiotic transporter activity / Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate / extrinsic component of membrane / porin activity / efflux transmembrane transporter activity / transmembrane transporter activity / monoatomic ion transmembrane transport / cell outer membrane / response to organic cyclic compound / response to toxic substance / monoatomic ion channel activity / outer membrane-bounded periplasmic space / response to xenobiotic stimulus / response to antibiotic / protein homodimerization activity / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Fitzpatrick, A.W.P. / Llabres, S. / Neuberger, A. / Blaza, J.N. / Bai, X.-C. / Okada, U. / Murakami, S. / van Veen, H.W. / Zachariae, U. / Scheres, S.H.W. ...Fitzpatrick, A.W.P. / Llabres, S. / Neuberger, A. / Blaza, J.N. / Bai, X.-C. / Okada, U. / Murakami, S. / van Veen, H.W. / Zachariae, U. / Scheres, S.H.W. / Luisi, B.F. / Du, D. | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump. Authors: Anthony W P Fitzpatrick / Salomé Llabrés / Arthur Neuberger / James N Blaza / Xiao-Chen Bai / Ui Okada / Satoshi Murakami / Hendrik W van Veen / Ulrich Zachariae / Sjors H W Scheres / Ben ...Authors: Anthony W P Fitzpatrick / Salomé Llabrés / Arthur Neuberger / James N Blaza / Xiao-Chen Bai / Ui Okada / Satoshi Murakami / Hendrik W van Veen / Ulrich Zachariae / Sjors H W Scheres / Ben F Luisi / Dijun Du / ![]() ![]() Abstract: 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 ...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. | |||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 828.9 KB | Display | ![]() |
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PDB format | ![]() | 690.8 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 740 KB | Display | ![]() |
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Full document | ![]() | 869.1 KB | Display | |
Data in XML | ![]() | 123.2 KB | Display | |
Data in CIF | ![]() | 188.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3652MC ![]() 3653C ![]() 5nilC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 52506.547 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: tolC, colE1-i, mtcB, mukA, refI, toc, weeA, b3035, JW5503 Production host: ![]() ![]() #2: Protein | Mass: 40715.746 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: macA, ybjY, b0878, JW0862 / Production host: ![]() ![]() #3: Protein | Mass: 71600.094 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: macB, ybjZ, b0879, JW0863 / Production host: ![]() ![]() References: UniProt: P75831, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: MacAB-TolC / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 27614 / Symmetry type: POINT |