Molecular and cellular dynamics of the 26S proteasome
| Autor: | Wolfgang Baumeister, Eri Sakata, Markus R. Eisele |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proteasome Endopeptidase Complex
0303 health sciences Protein Conformation Chemistry Cryo-electron microscopy Cryoelectron Microscopy Biophysics Single particle analysis Context (language use) Crystallography X-Ray Biochemistry Molecular machine Analytical Chemistry 03 medical and health sciences 0302 clinical medicine Proteasome Cryo-electron tomography Cellular dynamics Molecular Biology 030217 neurology & neurosurgery Subcellular Fractions 030304 developmental biology Macromolecule |
| Zdroj: | Biochimica et Biophysica Acta-Proteins and Proteomics |
| Popis: | In eukaryotic cells, the ubiquitin-proteasome system serves to remove proteins that are either dysfunctional or no longer needed. The 26S proteasome is a 2.5 MDa multisubunit complex comprising the 20S core particle, where degradation is executed, and one or two regulatory particles which prepare substrates for degradation. Whereas the 20S core particles of several species had been studied extensively by X-ray crystallography, the 26S holocomplex structure had remained elusive for a long time. Recent advances in single-particle cryo-electron microscopy have changed the situation and provided atomic resolution models of this intriguing molecular machine and its dynamics. Besides, cryo-electron tomography enables structural studies in situ, providing molecular resolution images of macromolecules inside pristinely preserved cellular environments. This has greatly contributed to our understanding of proteasome dynamics in the context of cells. |
| Databáze: | OpenAIRE |
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