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Cryo-EM structure of Neurospora crassa respiratory complex IV
In fungi, the mitochondrial respiratory chain complexes (complexes I–IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane protein from Neurospora crassa in lipid nanodiscs as cytochrome c oxidase (complex IV) and its structure wa...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6608615/ https://www.ncbi.nlm.nih.gov/pubmed/31316820 http://dx.doi.org/10.1107/S2052252519007486 |
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author | Bausewein, Thomas Nussberger, Stephan Kühlbrandt, Werner |
author_facet | Bausewein, Thomas Nussberger, Stephan Kühlbrandt, Werner |
author_sort | Bausewein, Thomas |
collection | PubMed |
description | In fungi, the mitochondrial respiratory chain complexes (complexes I–IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane protein from Neurospora crassa in lipid nanodiscs as cytochrome c oxidase (complex IV) and its structure was determined at 5.5 Å resolution. The map closely resembles the cryo-EM structure of complex IV from Saccharomyces cerevisiae. Its ten subunits are conserved in S. cerevisiae and Bos taurus, but other transmembrane subunits are missing. The different structure of the Cox5a subunit is typical for fungal complex IV and may affect the interaction with complex III in a respiratory supercomplex. Additional density was found between the matrix domains of the Cox4 and Cox5a subunits that appears to be specific to N. crassa. |
format | Online Article Text |
id | pubmed-6608615 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-66086152019-07-17 Cryo-EM structure of Neurospora crassa respiratory complex IV Bausewein, Thomas Nussberger, Stephan Kühlbrandt, Werner IUCrJ Research Papers In fungi, the mitochondrial respiratory chain complexes (complexes I–IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane protein from Neurospora crassa in lipid nanodiscs as cytochrome c oxidase (complex IV) and its structure was determined at 5.5 Å resolution. The map closely resembles the cryo-EM structure of complex IV from Saccharomyces cerevisiae. Its ten subunits are conserved in S. cerevisiae and Bos taurus, but other transmembrane subunits are missing. The different structure of the Cox5a subunit is typical for fungal complex IV and may affect the interaction with complex III in a respiratory supercomplex. Additional density was found between the matrix domains of the Cox4 and Cox5a subunits that appears to be specific to N. crassa. International Union of Crystallography 2019-06-26 /pmc/articles/PMC6608615/ /pubmed/31316820 http://dx.doi.org/10.1107/S2052252519007486 Text en © Thomas Bausewein et al. 2019 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Research Papers Bausewein, Thomas Nussberger, Stephan Kühlbrandt, Werner Cryo-EM structure of Neurospora crassa respiratory complex IV |
title | Cryo-EM structure of Neurospora crassa respiratory complex IV |
title_full | Cryo-EM structure of Neurospora crassa respiratory complex IV |
title_fullStr | Cryo-EM structure of Neurospora crassa respiratory complex IV |
title_full_unstemmed | Cryo-EM structure of Neurospora crassa respiratory complex IV |
title_short | Cryo-EM structure of Neurospora crassa respiratory complex IV |
title_sort | cryo-em structure of neurospora crassa respiratory complex iv |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6608615/ https://www.ncbi.nlm.nih.gov/pubmed/31316820 http://dx.doi.org/10.1107/S2052252519007486 |
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