Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival

Nishinaga et al. present structural characterization of the transcription regulator PefR from S. agalactiae in different states (apo-, DNAbound, heme-bound, CO-heme-bound and CN-heme-bound-PefRs). Structural comparison revealed that unique heme coordination controls structural rearrangement for the...

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Autores principales: Megumi Nishinaga, Hiroshi Sugimoto, Yudai Nishitani, Seina Nagai, Satoru Nagatoishi, Norifumi Muraki, Takehiko Tosha, Kouhei Tsumoto, Shigetoshi Aono, Yoshitsugu Shiro, Hitomi Sawai
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/07128172ea764ecdbc5f4b432580abbb
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spelling oai:doaj.org-article:07128172ea764ecdbc5f4b432580abbb2021-12-02T14:30:33ZHeme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival10.1038/s42003-021-01987-52399-3642https://doaj.org/article/07128172ea764ecdbc5f4b432580abbb2021-04-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01987-5https://doaj.org/toc/2399-3642Nishinaga et al. present structural characterization of the transcription regulator PefR from S. agalactiae in different states (apo-, DNAbound, heme-bound, CO-heme-bound and CN-heme-bound-PefRs). Structural comparison revealed that unique heme coordination controls structural rearrangement for the survival of the neonatal infection-causing hemolytic bacteria.Megumi NishinagaHiroshi SugimotoYudai NishitaniSeina NagaiSatoru NagatoishiNorifumi MurakiTakehiko ToshaKouhei TsumotoShigetoshi AonoYoshitsugu ShiroHitomi SawaiNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Megumi Nishinaga
Hiroshi Sugimoto
Yudai Nishitani
Seina Nagai
Satoru Nagatoishi
Norifumi Muraki
Takehiko Tosha
Kouhei Tsumoto
Shigetoshi Aono
Yoshitsugu Shiro
Hitomi Sawai
Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
description Nishinaga et al. present structural characterization of the transcription regulator PefR from S. agalactiae in different states (apo-, DNAbound, heme-bound, CO-heme-bound and CN-heme-bound-PefRs). Structural comparison revealed that unique heme coordination controls structural rearrangement for the survival of the neonatal infection-causing hemolytic bacteria.
format article
author Megumi Nishinaga
Hiroshi Sugimoto
Yudai Nishitani
Seina Nagai
Satoru Nagatoishi
Norifumi Muraki
Takehiko Tosha
Kouhei Tsumoto
Shigetoshi Aono
Yoshitsugu Shiro
Hitomi Sawai
author_facet Megumi Nishinaga
Hiroshi Sugimoto
Yudai Nishitani
Seina Nagai
Satoru Nagatoishi
Norifumi Muraki
Takehiko Tosha
Kouhei Tsumoto
Shigetoshi Aono
Yoshitsugu Shiro
Hitomi Sawai
author_sort Megumi Nishinaga
title Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
title_short Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
title_full Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
title_fullStr Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
title_full_unstemmed Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
title_sort heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/07128172ea764ecdbc5f4b432580abbb
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