Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation

Virulent type III secretion systems (T3SSs) or injectisomes enable pathogenic bacteria to inject effector proteins directly into the host cell cytoplasm. Structures of a needle complex engaged with the effector protein reveal the complete secretion channel and provide insights into the mechanism of...

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Autores principales: Sean Miletic, Dirk Fahrenkamp, Nikolaus Goessweiner-Mohr, Jiri Wald, Maurice Pantel, Oliver Vesper, Vadim Kotov, Thomas C. Marlovits
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/66891609afd94b18bb304e7a5fff8d52
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spelling oai:doaj.org-article:66891609afd94b18bb304e7a5fff8d522021-12-02T13:33:09ZSubstrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation10.1038/s41467-021-21143-12041-1723https://doaj.org/article/66891609afd94b18bb304e7a5fff8d522021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21143-1https://doaj.org/toc/2041-1723Virulent type III secretion systems (T3SSs) or injectisomes enable pathogenic bacteria to inject effector proteins directly into the host cell cytoplasm. Structures of a needle complex engaged with the effector protein reveal the complete secretion channel and provide insights into the mechanism of substrate translocation through T3SSs.Sean MileticDirk FahrenkampNikolaus Goessweiner-MohrJiri WaldMaurice PantelOliver VesperVadim KotovThomas C. MarlovitsNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Sean Miletic
Dirk Fahrenkamp
Nikolaus Goessweiner-Mohr
Jiri Wald
Maurice Pantel
Oliver Vesper
Vadim Kotov
Thomas C. Marlovits
Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
description Virulent type III secretion systems (T3SSs) or injectisomes enable pathogenic bacteria to inject effector proteins directly into the host cell cytoplasm. Structures of a needle complex engaged with the effector protein reveal the complete secretion channel and provide insights into the mechanism of substrate translocation through T3SSs.
format article
author Sean Miletic
Dirk Fahrenkamp
Nikolaus Goessweiner-Mohr
Jiri Wald
Maurice Pantel
Oliver Vesper
Vadim Kotov
Thomas C. Marlovits
author_facet Sean Miletic
Dirk Fahrenkamp
Nikolaus Goessweiner-Mohr
Jiri Wald
Maurice Pantel
Oliver Vesper
Vadim Kotov
Thomas C. Marlovits
author_sort Sean Miletic
title Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
title_short Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
title_full Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
title_fullStr Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
title_full_unstemmed Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
title_sort substrate-engaged type iii secretion system structures reveal gating mechanism for unfolded protein translocation
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/66891609afd94b18bb304e7a5fff8d52
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