Journal
CURRENT RESEARCH IN STRUCTURAL BIOLOGY
Volume 1, Issue -, Pages 13-20Publisher
ELSEVIER
DOI: 10.1016/j.crstbi.2019.10.001
Keywords
AAA(+) proteins; ATPase module; Lon protease; Cryo-EM
Funding
- Frederick National Laboratory for Cancer Research, National Institutes of Health [HHSN261200800001E]
- NIH, National Cancer Institute, Center for Cancer Research
- Russian Foundation for Basic Research [19-04-00646]
Ask authors/readers for more resources
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 A. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available