3K1J

Crystal structure of Lon protease from Thermococcus onnurineus NA1

3K1J の概要

• エントリーDOI: 10.2210/pdb3k1j/pdb
• 分子名称: ATP-dependent protease Lon, ADENOSINE-5'-DIPHOSPHATE, 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL, ... (5 entities in total)
• 機能のキーワード: atp-dependent protease, atp-binding, nucleotide-binding, protease, hydrolase
• 由来する生物種: Thermococcus onnurineus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 135141.24

構造登録者

Cha, S.S.,An, Y.J. (登録日: 2009-09-28, 公開日: 2010-09-22, 最終更新日: 2024-10-30)

主引用文献

Cha, S.S.,An, Y.J.,Lee, C.R.,Lee, H.S.,Kim, Y.G.,Kim, S.J.,Kwon, K.K.,De Donatis, G.M.,Lee, J.H.,Maurizi, M.R.,Kang, S.G.
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber
Embo J., 29:3520-3530, 2010

PubMed Abstract: 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 domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions.

PubMed: 20834233
DOI: 10.1038/emboj.2010.226

実験手法

X-RAY DIFFRACTION (2 Å)