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ABC Transporters in Bacterial Nanomachineries
Members of the superfamily of ABC transporters are found in all domains of life. Most of these primary active transporters act as isolated entities and export or import their substrates in an ATP-dependent manner across biological membranes. However, some ABC transporters are also part of larger pro...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10094684/ https://www.ncbi.nlm.nih.gov/pubmed/37047196 http://dx.doi.org/10.3390/ijms24076227 |
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author | Bilsing, Florestan L. Anlauf, Manuel T. Hachani, Eymen Khosa, Sakshi Schmitt, Lutz |
author_facet | Bilsing, Florestan L. Anlauf, Manuel T. Hachani, Eymen Khosa, Sakshi Schmitt, Lutz |
author_sort | Bilsing, Florestan L. |
collection | PubMed |
description | Members of the superfamily of ABC transporters are found in all domains of life. Most of these primary active transporters act as isolated entities and export or import their substrates in an ATP-dependent manner across biological membranes. However, some ABC transporters are also part of larger protein complexes, so-called nanomachineries that catalyze the vectorial transport of their substrates. Here, we will focus on four bacterial examples of such nanomachineries: the Mac system providing drug resistance, the Lpt system catalyzing vectorial LPS transport, the Mla system responsible for phospholipid transport, and the Lol system, which is required for lipoprotein transport to the outer membrane of Gram-negative bacteria. For all four systems, we tried to summarize the existing data and provide a structure-function analysis highlighting the mechanistical aspect of the coupling of ATP hydrolysis to substrate translocation. |
format | Online Article Text |
id | pubmed-10094684 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100946842023-04-13 ABC Transporters in Bacterial Nanomachineries Bilsing, Florestan L. Anlauf, Manuel T. Hachani, Eymen Khosa, Sakshi Schmitt, Lutz Int J Mol Sci Review Members of the superfamily of ABC transporters are found in all domains of life. Most of these primary active transporters act as isolated entities and export or import their substrates in an ATP-dependent manner across biological membranes. However, some ABC transporters are also part of larger protein complexes, so-called nanomachineries that catalyze the vectorial transport of their substrates. Here, we will focus on four bacterial examples of such nanomachineries: the Mac system providing drug resistance, the Lpt system catalyzing vectorial LPS transport, the Mla system responsible for phospholipid transport, and the Lol system, which is required for lipoprotein transport to the outer membrane of Gram-negative bacteria. For all four systems, we tried to summarize the existing data and provide a structure-function analysis highlighting the mechanistical aspect of the coupling of ATP hydrolysis to substrate translocation. MDPI 2023-03-25 /pmc/articles/PMC10094684/ /pubmed/37047196 http://dx.doi.org/10.3390/ijms24076227 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Bilsing, Florestan L. Anlauf, Manuel T. Hachani, Eymen Khosa, Sakshi Schmitt, Lutz ABC Transporters in Bacterial Nanomachineries |
title | ABC Transporters in Bacterial Nanomachineries |
title_full | ABC Transporters in Bacterial Nanomachineries |
title_fullStr | ABC Transporters in Bacterial Nanomachineries |
title_full_unstemmed | ABC Transporters in Bacterial Nanomachineries |
title_short | ABC Transporters in Bacterial Nanomachineries |
title_sort | abc transporters in bacterial nanomachineries |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10094684/ https://www.ncbi.nlm.nih.gov/pubmed/37047196 http://dx.doi.org/10.3390/ijms24076227 |
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