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Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex
The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to sel...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7251119/ https://www.ncbi.nlm.nih.gov/pubmed/32457311 http://dx.doi.org/10.1038/s41467-020-16397-0 |
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author | Kim, Hyunmin Kubori, Tomoko Yamazaki, Kohei Kwak, Mi-Jeong Park, Suk-Youl Nagai, Hiroki Vogel, Joseph P. Oh, Byung-Ha |
author_facet | Kim, Hyunmin Kubori, Tomoko Yamazaki, Kohei Kwak, Mi-Jeong Park, Suk-Youl Nagai, Hiroki Vogel, Joseph P. Oh, Byung-Ha |
author_sort | Kim, Hyunmin |
collection | PubMed |
description | The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to selectively assist the export of a subclass of effectors. Herein, the crystal structure of a four-subunit T4CP subcomplex bound to the effector protein VpdB reveals an interaction between LvgA and a linear motif in the C-terminus of VpdB. The same binding interface of LvgA also interacts with the C-terminal region of three additional effectors, SidH, SetA and PieA. Mutational analyses identified a FxxxLxxxK binding motif that is shared by VpdB and SidH, but not by SetA and PieA, showing that LvgA recognizes more than one type of binding motif. Together, this work provides a structural basis for how the Dot/Icm T4CP complex recognizes effectors, and highlights the multiple substrate-binding specificities of its adaptor subunit. |
format | Online Article Text |
id | pubmed-7251119 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72511192020-06-04 Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex Kim, Hyunmin Kubori, Tomoko Yamazaki, Kohei Kwak, Mi-Jeong Park, Suk-Youl Nagai, Hiroki Vogel, Joseph P. Oh, Byung-Ha Nat Commun Article The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to selectively assist the export of a subclass of effectors. Herein, the crystal structure of a four-subunit T4CP subcomplex bound to the effector protein VpdB reveals an interaction between LvgA and a linear motif in the C-terminus of VpdB. The same binding interface of LvgA also interacts with the C-terminal region of three additional effectors, SidH, SetA and PieA. Mutational analyses identified a FxxxLxxxK binding motif that is shared by VpdB and SidH, but not by SetA and PieA, showing that LvgA recognizes more than one type of binding motif. Together, this work provides a structural basis for how the Dot/Icm T4CP complex recognizes effectors, and highlights the multiple substrate-binding specificities of its adaptor subunit. Nature Publishing Group UK 2020-05-26 /pmc/articles/PMC7251119/ /pubmed/32457311 http://dx.doi.org/10.1038/s41467-020-16397-0 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Kim, Hyunmin Kubori, Tomoko Yamazaki, Kohei Kwak, Mi-Jeong Park, Suk-Youl Nagai, Hiroki Vogel, Joseph P. Oh, Byung-Ha Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title | Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title_full | Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title_fullStr | Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title_full_unstemmed | Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title_short | Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex |
title_sort | structural basis for effector protein recognition by the dot/icm type ivb coupling protein complex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7251119/ https://www.ncbi.nlm.nih.gov/pubmed/32457311 http://dx.doi.org/10.1038/s41467-020-16397-0 |
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