title: Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH.
abstract: When bound to ADP, ATP-dependent protease FtsH subunits adopt either an "open" or "closed" conformation. In the open state, the protease catalytic site is located in a narrow space covered by a lidlike helix. This space disappears in the closed form because the lid helix bends at Gly448. Here, we replaced Gly448 with various residues that stabilize helices. Most mutants retained low ATPase activity and bound to the substrate protein, but lost protease activity. However, a mutant proline substitution lost both activities. Our study shows that the conformational transition of the lid helix is essential for the function of FtsH.
authors.affiliation: Department of Molecular Bioscience, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
authors.forename: Ryoji
authors.initials: R
authors.lastname: Suno
authors.forename: Masakazu
authors.initials: M
authors.lastname: Shimoyama
authors.forename: Akiko
authors.initials: A
authors.lastname: Abe
authors.forename: Tatsuro
authors.initials: T
authors.lastname: Shimamura
authors.forename: Natsuka
authors.initials: N
authors.lastname: Shimodate
authors.forename: Yo-hei
authors.initials: YH
authors.lastname: Watanabe
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Akiyama
authors.forename: Masasuke
authors.initials: M
authors.lastname: Yoshida
mesh_terms: D049069:ATP-Dependent Proteases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D050505:Mutant Proteins; D011994:Recombinant Proteins; D049069:ATP-Dependent Proteases