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Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry
The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome’s structure has been known for some years, the highly dynamic nature of the 19S regulatory particl...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8067131/ https://www.ncbi.nlm.nih.gov/pubmed/33801594 http://dx.doi.org/10.3390/biom11040505 |
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author | Mendes, Marta L. Dittmar, Gunnar |
author_facet | Mendes, Marta L. Dittmar, Gunnar |
author_sort | Mendes, Marta L. |
collection | PubMed |
description | The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome’s structure has been known for some years, the highly dynamic nature of the 19S regulatory particle has presented a challenge to structural biologists. Advances in cryo-electron microscopy (cryo-EM) made it possible to determine the structure of the 19S regulatory particle and showed at least seven different conformational states of the proteasome. However, there are still many questions to be answered. Cross-linking mass spectrometry (CLMS) is now routinely used in integrative structural biology studies, and it promises to take integrative structural biology to the next level, answering some of these questions. |
format | Online Article Text |
id | pubmed-8067131 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80671312021-04-25 Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry Mendes, Marta L. Dittmar, Gunnar Biomolecules Perspective The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome’s structure has been known for some years, the highly dynamic nature of the 19S regulatory particle has presented a challenge to structural biologists. Advances in cryo-electron microscopy (cryo-EM) made it possible to determine the structure of the 19S regulatory particle and showed at least seven different conformational states of the proteasome. However, there are still many questions to be answered. Cross-linking mass spectrometry (CLMS) is now routinely used in integrative structural biology studies, and it promises to take integrative structural biology to the next level, answering some of these questions. MDPI 2021-03-27 /pmc/articles/PMC8067131/ /pubmed/33801594 http://dx.doi.org/10.3390/biom11040505 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Perspective Mendes, Marta L. Dittmar, Gunnar Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title | Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title_full | Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title_fullStr | Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title_full_unstemmed | Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title_short | Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry |
title_sort | analysis of the dynamic proteasome structure by cross-linking mass spectrometry |
topic | Perspective |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8067131/ https://www.ncbi.nlm.nih.gov/pubmed/33801594 http://dx.doi.org/10.3390/biom11040505 |
work_keys_str_mv | AT mendesmartal analysisofthedynamicproteasomestructurebycrosslinkingmassspectrometry AT dittmargunnar analysisofthedynamicproteasomestructurebycrosslinkingmassspectrometry |