Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
The MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2018-05-01
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| Series: | Frontiers in Microbiology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2018.00950/full |
| _version_ | 1818506393148194816 |
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| author | Nicholas P. Greene Elise Kaplan Allister Crow Vassilis Koronakis |
| author_facet | Nicholas P. Greene Elise Kaplan Allister Crow Vassilis Koronakis |
| author_sort | Nicholas P. Greene |
| collection | DOAJ |
| description | The MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that is distinct from other structurally characterized ABC transporters and uses a unique molecular mechanism termed mechanotransmission. Unlike other bacterial ABC transporters, MacB does not transport substrates across the inner membrane in which it is based, but instead couples cytoplasmic ATP hydrolysis with transmembrane conformational changes that are used to perform work in the extra-cytoplasmic space. In the MacAB-TolC tripartite pump, mechanotransmission drives efflux of antibiotics and export of a protein toxin from the periplasmic space via the TolC exit duct. Homologous tripartite systems from pathogenic bacteria similarly export protein-like signaling molecules, virulence factors and siderophores. In addition, many MacB-like ABC transporters do not form tripartite pumps, but instead operate in diverse cellular processes including antibiotic sensing, cell division and lipoprotein trafficking. |
| first_indexed | 2024-12-10T22:03:57Z |
| format | Article |
| id | doaj.art-29beaa292c1a40189cfbf14fd8fb5739 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-10T22:03:57Z |
| publishDate | 2018-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-29beaa292c1a40189cfbf14fd8fb57392022-12-22T01:31:48ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2018-05-01910.3389/fmicb.2018.00950369512Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional PerspectiveNicholas P. Greene0Elise Kaplan1Allister Crow2Vassilis Koronakis3Department of Pathology, University of Cambridge, Cambridge, United KingdomDepartment of Pathology, University of Cambridge, Cambridge, United KingdomSchool of Life Sciences, University of Warwick, Coventry, United KingdomDepartment of Pathology, University of Cambridge, Cambridge, United KingdomThe MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that is distinct from other structurally characterized ABC transporters and uses a unique molecular mechanism termed mechanotransmission. Unlike other bacterial ABC transporters, MacB does not transport substrates across the inner membrane in which it is based, but instead couples cytoplasmic ATP hydrolysis with transmembrane conformational changes that are used to perform work in the extra-cytoplasmic space. In the MacAB-TolC tripartite pump, mechanotransmission drives efflux of antibiotics and export of a protein toxin from the periplasmic space via the TolC exit duct. Homologous tripartite systems from pathogenic bacteria similarly export protein-like signaling molecules, virulence factors and siderophores. In addition, many MacB-like ABC transporters do not form tripartite pumps, but instead operate in diverse cellular processes including antibiotic sensing, cell division and lipoprotein trafficking.https://www.frontiersin.org/article/10.3389/fmicb.2018.00950/fullantibiotic resistancetripartite efflux pumpMacBmechanotransmissionABC transporterlantibiotic |
| spellingShingle | Nicholas P. Greene Elise Kaplan Allister Crow Vassilis Koronakis Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective Frontiers in Microbiology antibiotic resistance tripartite efflux pump MacB mechanotransmission ABC transporter lantibiotic |
| title | Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective |
| title_full | Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective |
| title_fullStr | Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective |
| title_full_unstemmed | Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective |
| title_short | Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective |
| title_sort | antibiotic resistance mediated by the macb abc transporter family a structural and functional perspective |
| topic | antibiotic resistance tripartite efflux pump MacB mechanotransmission ABC transporter lantibiotic |
| url | https://www.frontiersin.org/article/10.3389/fmicb.2018.00950/full |
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