4EIW

Whole cytosolic region of atp-dependent metalloprotease FtsH (G399L)

4EIW の概要

• エントリーDOI: 10.2210/pdb4eiw/pdb
• 分子名称: ATP-dependent zinc metalloprotease FtsH, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: walker motif, atpase, hydrolase
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cell inner membrane (Probable); Multi-pass membrane protein; Cytoplasmic side (By similarity): Q5SI82
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 339632.50

構造登録者

Suno, R.,Niwa, H.,Tsuchiya, D.,Yoshida, M.,Morikawa, K. (登録日: 2012-04-06, 公開日: 2012-06-06, 最終更新日: 2024-03-20)

主引用文献

Suno, R.,Niwa, H.,Tsuchiya, D.,Zhang, X.,Yoshida, M.,Morikawa, K.
Structure of the whole cytosolic region of ATP-dependent protease FtsH
Mol.Cell, 22:575-585, 2006

PubMed Abstract: An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.

PubMed: 16762831
DOI: 10.1016/j.molcel.2006.04.020

実験手法

X-RAY DIFFRACTION (3.9 Å)