| Autor: |
Istvan Botos, George T. Lountos, Weimin Wu, Scott Cherry, Rodolfo Ghirlando, Arsen M. Kudzhaev, Tatyana V. Rotanova, Natalia de Val, Joseph E. Tropea, Alla Gustchina, Alexander Wlodawer |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| Předmět: |
|
| Zdroj: |
Current Research in Structural Biology, Vol 1, Iss , Pp 13-20 (2019) |
| Druh dokumentu: |
article |
| ISSN: |
2665-928X |
| DOI: |
10.1016/j.crstbi.2019.10.001 |
| Popis: |
Energy-dependent Lon proteases play a key role in cellular regulation by degrading short-lived regulatory proteins and misfolded proteins in the cell. The structure of the catalytically inactive S679A mutant of Escherichia coli LonA protease (EcLon) has been determined by cryo-EM at the resolution of 3.5 Å. EcLonA without a bound substrate adopts a hexameric open-spiral quaternary structure that might represent the resting state of the enzyme. Upon interaction with substrate the open-spiral hexamer undergoes a major conformational change resulting in a compact, closed-circle hexamer as in the recent structure of a complex of Yersinia pestis LonA with a protein substrate. This major change is accomplished by the rigid-body rearrangement of the individual domains within the protomers of the complex around the hinge points in the interdomain linkers. Comparison of substrate-free and substrate-bound Lon structures allows to mark the location of putative pivotal points involved in such conformational changes. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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