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Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex
Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1–reaction center (LH1–RC) complex, but lacks protein-U, a U-shaped polypeptide in the L...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9932092/ https://www.ncbi.nlm.nih.gov/pubmed/36792596 http://dx.doi.org/10.1038/s41467-023-36460-w |
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author | Tani, Kazutoshi Kanno, Ryo Ji, Xuan-Cheng Satoh, Itsusei Kobayashi, Yuki Hall, Malgorzata Yu, Long-Jiang Kimura, Yukihiro Mizoguchi, Akira Humbel, Bruno M. Madigan, Michael T. Wang-Otomo, Zheng-Yu |
author_facet | Tani, Kazutoshi Kanno, Ryo Ji, Xuan-Cheng Satoh, Itsusei Kobayashi, Yuki Hall, Malgorzata Yu, Long-Jiang Kimura, Yukihiro Mizoguchi, Akira Humbel, Bruno M. Madigan, Michael T. Wang-Otomo, Zheng-Yu |
author_sort | Tani, Kazutoshi |
collection | PubMed |
description | Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1–reaction center (LH1–RC) complex, but lacks protein-U, a U-shaped polypeptide in the LH1–RC of its close relative Rba. sphaeroides. Here we present a cryo-EM structure of the Rba. capsulatus LH1–RC purified by DEAE chromatography. The crescent-shaped LH1–RC exhibits a compact structure containing only 10 LH1 αβ-subunits. Four αβ-subunits corresponding to those adjacent to protein-U in Rba. sphaeroides were absent. PufX in Rba. capsulatus exhibits a unique conformation in its N-terminus that self-associates with amino acids in its own transmembrane domain and interacts with nearby polypeptides, preventing it from interacting with proteins in other complexes and forming dimeric structures. These features are discussed in relation to the minimal requirements for the formation of LH1–RC monomers and dimers, the spectroscopic behavior of both the LH1 and RC, and the bioenergetics of energy transfer from LH1 to the RC. |
format | Online Article Text |
id | pubmed-9932092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-99320922023-02-17 Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex Tani, Kazutoshi Kanno, Ryo Ji, Xuan-Cheng Satoh, Itsusei Kobayashi, Yuki Hall, Malgorzata Yu, Long-Jiang Kimura, Yukihiro Mizoguchi, Akira Humbel, Bruno M. Madigan, Michael T. Wang-Otomo, Zheng-Yu Nat Commun Article Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1–reaction center (LH1–RC) complex, but lacks protein-U, a U-shaped polypeptide in the LH1–RC of its close relative Rba. sphaeroides. Here we present a cryo-EM structure of the Rba. capsulatus LH1–RC purified by DEAE chromatography. The crescent-shaped LH1–RC exhibits a compact structure containing only 10 LH1 αβ-subunits. Four αβ-subunits corresponding to those adjacent to protein-U in Rba. sphaeroides were absent. PufX in Rba. capsulatus exhibits a unique conformation in its N-terminus that self-associates with amino acids in its own transmembrane domain and interacts with nearby polypeptides, preventing it from interacting with proteins in other complexes and forming dimeric structures. These features are discussed in relation to the minimal requirements for the formation of LH1–RC monomers and dimers, the spectroscopic behavior of both the LH1 and RC, and the bioenergetics of energy transfer from LH1 to the RC. Nature Publishing Group UK 2023-02-15 /pmc/articles/PMC9932092/ /pubmed/36792596 http://dx.doi.org/10.1038/s41467-023-36460-w Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Tani, Kazutoshi Kanno, Ryo Ji, Xuan-Cheng Satoh, Itsusei Kobayashi, Yuki Hall, Malgorzata Yu, Long-Jiang Kimura, Yukihiro Mizoguchi, Akira Humbel, Bruno M. Madigan, Michael T. Wang-Otomo, Zheng-Yu Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title | Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title_full | Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title_fullStr | Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title_full_unstemmed | Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title_short | Rhodobacter capsulatus forms a compact crescent-shaped LH1–RC photocomplex |
title_sort | rhodobacter capsulatus forms a compact crescent-shaped lh1–rc photocomplex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9932092/ https://www.ncbi.nlm.nih.gov/pubmed/36792596 http://dx.doi.org/10.1038/s41467-023-36460-w |
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