Molecular architecture and the mechanics of Lon, a protease-chaperone machine

Title
Molecular architecture and the mechanics of Lon, a protease-chaperone machine
Author(s)
차선신
Publication Year
2010-05-06
Abstract
The ATP-dependent Lon protease, which has orthologs distributed in all kingdoms of life, is essential in bacteria and other microorganisms under stress conditions and is needed for survival of mammalian cells subjected to oxidative damage. Lon consists of a molecular chaperone belonging to the AAA+ family and a protease with a serine-lysine catalytic dyad encoded in tandem in a single polypeptide. Here, we report the 2.0 ?resolution crystal structure of Lon from Thermococcus onnurineus NA14 (TonLon). Six subunits of TonLon assemble into a cylindrical structure with a sequestered internal chamber harboring the proteolytic active sites accessible only through restricted axial channels. Alternating subunits exist in two different nucleotide states displaying different domain orientations and intersubunit contacts indicative of the ATP hydrolysis-coupled motions driving protein unfolding and translocation.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/28997
Bibliographic Citation
2010 International Meeting of the Microbiological Society of Korea, pp.96, 2010
Publisher
The Microbiological Society of Korea
Type
Conference
Language
English
Publisher
The Microbiological Society of Korea
Files in This Item:
There are no files associated with this item.

qrcode

Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse