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Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar...

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Autores principales: Kawakami, Tomoaki, Yu, Long-Jiang, Liang, Tai, Okazaki, Koudai, Madigan, Michael T., Kimura, Yukihiro, Wang-Otomo, Zheng-Yu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7889895/
https://www.ncbi.nlm.nih.gov/pubmed/33597527
http://dx.doi.org/10.1038/s41467-021-21397-9
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author Kawakami, Tomoaki
Yu, Long-Jiang
Liang, Tai
Okazaki, Koudai
Madigan, Michael T.
Kimura, Yukihiro
Wang-Otomo, Zheng-Yu
author_facet Kawakami, Tomoaki
Yu, Long-Jiang
Liang, Tai
Okazaki, Koudai
Madigan, Michael T.
Kimura, Yukihiro
Wang-Otomo, Zheng-Yu
author_sort Kawakami, Tomoaki
collection PubMed
description Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems.
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spelling pubmed-78898952021-03-03 Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP Kawakami, Tomoaki Yu, Long-Jiang Liang, Tai Okazaki, Koudai Madigan, Michael T. Kimura, Yukihiro Wang-Otomo, Zheng-Yu Nat Commun Article Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems. Nature Publishing Group UK 2021-02-17 /pmc/articles/PMC7889895/ /pubmed/33597527 http://dx.doi.org/10.1038/s41467-021-21397-9 Text en © The Author(s) 2021 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
Kawakami, Tomoaki
Yu, Long-Jiang
Liang, Tai
Okazaki, Koudai
Madigan, Michael T.
Kimura, Yukihiro
Wang-Otomo, Zheng-Yu
Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_full Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_fullStr Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_full_unstemmed Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_short Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_sort crystal structure of a photosynthetic lh1-rc in complex with its electron donor hipip
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7889895/
https://www.ncbi.nlm.nih.gov/pubmed/33597527
http://dx.doi.org/10.1038/s41467-021-21397-9
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