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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...

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Detalles Bibliográficos
Autores principales: Mendes, Marta L., Dittmar, Gunnar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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.
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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
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