Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing
Proteasomal ATPases contain functionally important coiled-coil (CC) domains, the mechanistic role of which is not fully understood. Here, the authors provide evidence for three distinct CC conformations, showing that CC conformational changes enable ATPases to switch between active and resting state...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2018-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-04731-6 |
| Summary: | Proteasomal ATPases contain functionally important coiled-coil (CC) domains, the mechanistic role of which is not fully understood. Here, the authors provide evidence for three distinct CC conformations, showing that CC conformational changes enable ATPases to switch between active and resting states. |
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| ISSN: | 2041-1723 |