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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| Format: | Article |
| Language: | English |
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MDPI AG
2021-03-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/4/505 |
| _version_ | 1797539857425235968 |
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| author | Marta L. Mendes Gunnar Dittmar |
| author_facet | Marta L. Mendes Gunnar Dittmar |
| author_sort | Marta L. Mendes |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T12:51:51Z |
| format | Article |
| id | doaj.art-fdffd3e66edc49faab10bda01229de26 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T12:51:51Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-fdffd3e66edc49faab10bda01229de262023-11-21T13:02:40ZengMDPI AGBiomolecules2218-273X2021-03-0111450510.3390/biom11040505Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass SpectrometryMarta L. Mendes0Gunnar Dittmar1Proteomics of Cellular Signaling, Department of Infection and Immunity, Luxembourg Institute of Health, 1a Rue Thomas Edison, 1445 Strassen, LuxembourgProteomics of Cellular Signaling, Department of Infection and Immunity, Luxembourg Institute of Health, 1a Rue Thomas Edison, 1445 Strassen, LuxembourgThe 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.https://www.mdpi.com/2218-273X/11/4/505proteasomecross-linking mass spectrometrystructural biologyX-ray crystallographyelectron microscopy |
| spellingShingle | Marta L. Mendes Gunnar Dittmar Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry Biomolecules proteasome cross-linking mass spectrometry structural biology X-ray crystallography electron microscopy |
| 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 | proteasome cross-linking mass spectrometry structural biology X-ray crystallography electron microscopy |
| url | https://www.mdpi.com/2218-273X/11/4/505 |
| work_keys_str_mv | AT martalmendes analysisofthedynamicproteasomestructurebycrosslinkingmassspectrometry AT gunnardittmar analysisofthedynamicproteasomestructurebycrosslinkingmassspectrometry |