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Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria
[Image: see text] Tripartite efflux pumps and the related type 1 secretion systems (T1SSs) in Gram-negative organisms are diverse in function, energization, and structural organization. They form continuous conduits spanning both the inner and the outer membrane and are composed of three principal c...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8277102/ https://www.ncbi.nlm.nih.gov/pubmed/33909410 http://dx.doi.org/10.1021/acs.chemrev.1c00055 |
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author | Alav, Ilyas Kobylka, Jessica Kuth, Miriam S. Pos, Klaas M. Picard, Martin Blair, Jessica M. A. Bavro, Vassiliy N. |
author_facet | Alav, Ilyas Kobylka, Jessica Kuth, Miriam S. Pos, Klaas M. Picard, Martin Blair, Jessica M. A. Bavro, Vassiliy N. |
author_sort | Alav, Ilyas |
collection | PubMed |
description | [Image: see text] Tripartite efflux pumps and the related type 1 secretion systems (T1SSs) in Gram-negative organisms are diverse in function, energization, and structural organization. They form continuous conduits spanning both the inner and the outer membrane and are composed of three principal components—the energized inner membrane transporters (belonging to ABC, RND, and MFS families), the outer membrane factor channel-like proteins, and linking the two, the periplasmic adaptor proteins (PAPs), also known as the membrane fusion proteins (MFPs). In this review we summarize the recent advances in understanding of structural biology, function, and regulation of these systems, highlighting the previously undescribed role of PAPs in providing a common architectural scaffold across diverse families of transporters. Despite being built from a limited number of basic structural domains, these complexes present a staggering variety of architectures. While key insights have been derived from the RND transporter systems, a closer inspection of the operation and structural organization of different tripartite systems reveals unexpected analogies between them, including those formed around MFS- and ATP-driven transporters, suggesting that they operate around basic common principles. Based on that we are proposing a new integrated model of PAP-mediated communication within the conformational cycling of tripartite systems, which could be expanded to other types of assemblies. |
format | Online Article Text |
id | pubmed-8277102 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-82771022021-07-14 Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria Alav, Ilyas Kobylka, Jessica Kuth, Miriam S. Pos, Klaas M. Picard, Martin Blair, Jessica M. A. Bavro, Vassiliy N. Chem Rev [Image: see text] Tripartite efflux pumps and the related type 1 secretion systems (T1SSs) in Gram-negative organisms are diverse in function, energization, and structural organization. They form continuous conduits spanning both the inner and the outer membrane and are composed of three principal components—the energized inner membrane transporters (belonging to ABC, RND, and MFS families), the outer membrane factor channel-like proteins, and linking the two, the periplasmic adaptor proteins (PAPs), also known as the membrane fusion proteins (MFPs). In this review we summarize the recent advances in understanding of structural biology, function, and regulation of these systems, highlighting the previously undescribed role of PAPs in providing a common architectural scaffold across diverse families of transporters. Despite being built from a limited number of basic structural domains, these complexes present a staggering variety of architectures. While key insights have been derived from the RND transporter systems, a closer inspection of the operation and structural organization of different tripartite systems reveals unexpected analogies between them, including those formed around MFS- and ATP-driven transporters, suggesting that they operate around basic common principles. Based on that we are proposing a new integrated model of PAP-mediated communication within the conformational cycling of tripartite systems, which could be expanded to other types of assemblies. American Chemical Society 2021-04-28 2021-05-12 /pmc/articles/PMC8277102/ /pubmed/33909410 http://dx.doi.org/10.1021/acs.chemrev.1c00055 Text en © 2021 The Authors. Published by American Chemical Society Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Alav, Ilyas Kobylka, Jessica Kuth, Miriam S. Pos, Klaas M. Picard, Martin Blair, Jessica M. A. Bavro, Vassiliy N. Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria |
title | Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria |
title_full | Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria |
title_fullStr | Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria |
title_full_unstemmed | Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria |
title_short | Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria |
title_sort | structure, assembly, and function of tripartite efflux
and type 1 secretion systems in gram-negative bacteria |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8277102/ https://www.ncbi.nlm.nih.gov/pubmed/33909410 http://dx.doi.org/10.1021/acs.chemrev.1c00055 |
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