Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring

The bacterial flagellum is a motility organelle formed by tens of thousands of protein molecules. At the earliest stage of flagellar assembly, a transmembrane protein, FliF, forms the MS-ring in the cytoplasmic membrane as the base for flagellar assembly.

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Autores principales: Norihiro Takekawa, Akihiro Kawamoto, Mayuko Sakuma, Takayuki Kato, Seiji Kojima, Miki Kinoshita, Tohru Minamino, Keiichi Namba, Michio Homma, Katsumi Imada
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Publicado: American Society for Microbiology 2021
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Acceso en línea:https://doaj.org/article/f5c71112b105479b824c20f8447b455b
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spelling oai:doaj.org-article:f5c71112b105479b824c20f8447b455b2021-11-03T18:56:09ZTwo Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring2150-751110.1128/mBio.03199-20https://doaj.org/article/f5c71112b105479b824c20f8447b455b2021-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.03199-20https://doaj.org/toc/2150-7511 The bacterial flagellum is a motility organelle formed by tens of thousands of protein molecules. At the earliest stage of flagellar assembly, a transmembrane protein, FliF, forms the MS-ring in the cytoplasmic membrane as the base for flagellar assembly.Norihiro TakekawaAkihiro KawamotoMayuko SakumaTakayuki KatoSeiji KojimaMiki KinoshitaTohru MinaminoKeiichi NambaMichio HommaKatsumi ImadaAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 12, Iss 2 (2021)
institution DOAJ
collection DOAJ
language EN
topic Microbiology
QR1-502
spellingShingle Microbiology
QR1-502
Norihiro Takekawa
Akihiro Kawamoto
Mayuko Sakuma
Takayuki Kato
Seiji Kojima
Miki Kinoshita
Tohru Minamino
Keiichi Namba
Michio Homma
Katsumi Imada
Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
description The bacterial flagellum is a motility organelle formed by tens of thousands of protein molecules. At the earliest stage of flagellar assembly, a transmembrane protein, FliF, forms the MS-ring in the cytoplasmic membrane as the base for flagellar assembly.
format article
author Norihiro Takekawa
Akihiro Kawamoto
Mayuko Sakuma
Takayuki Kato
Seiji Kojima
Miki Kinoshita
Tohru Minamino
Keiichi Namba
Michio Homma
Katsumi Imada
author_facet Norihiro Takekawa
Akihiro Kawamoto
Mayuko Sakuma
Takayuki Kato
Seiji Kojima
Miki Kinoshita
Tohru Minamino
Keiichi Namba
Michio Homma
Katsumi Imada
author_sort Norihiro Takekawa
title Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
title_short Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
title_full Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
title_fullStr Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
title_full_unstemmed Two Distinct Conformations in 34 FliF Subunits Generate Three Different Symmetries within the Flagellar MS-Ring
title_sort two distinct conformations in 34 flif subunits generate three different symmetries within the flagellar ms-ring
publisher American Society for Microbiology
publishDate 2021
url https://doaj.org/article/f5c71112b105479b824c20f8447b455b
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AT michiohomma twodistinctconformationsin34flifsubunitsgeneratethreedifferentsymmetrieswithintheflagellarmsring
AT katsumiimada twodistinctconformationsin34flifsubunitsgeneratethreedifferentsymmetrieswithintheflagellarmsring
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