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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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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. |
format | Online Article Text |
id | pubmed-7889895 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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