| Autor: |
Botos, Istvan, Lountos, George T., Wu, Weimin, Cherry, Scott, Ghirlando, Rodolfo, Kudzhaev, Arsen M., Rotanova, Tatyana V., de Val, Natalia, Tropea, Joseph E., Gustchina, Alla, Wlodawer, Alexander |
| Zdroj: |
Current Research in Structural Biology; November 2019, Vol. 1 Issue: 1 p13-20, 8p |
| Abstrakt: |
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 coliLonA 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 pestisLonA 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: |
Supplemental Index |
| Externí odkaz: |
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