Ontology highlight
ABSTRACT:
SUBMITTER: Cha SS
PROVIDER: S-EPMC2964173 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Cha Sun-Shin SS An Young Jun YJ Lee Chang Ro CR Lee Hyun Sook HS Kim Yeon-Gil YG Kim Sang Jin SJ Kwon Kae Kyoung KK De Donatis Gian Marco GM Lee Jung-Hyun JH Maurizi Michael R MR Kang Sung Gyun SG
The EMBO journal 20100910 20
Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-Å resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion ...[more]