Structural studies on Helicobacter pylori ATP-dependent protease, FtsH

• Published in: Journal of synchrotron radiation Vol. 15; no. 3; pp. 208 - 210
• Main Authors: Kim, Sung Hyun, Kang, Gil Bu, Song, Hye-Eun, Park, Sang Jin, Bea, Man-Ho, Eom, Soo Hyun
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.05.2008
• Subjects: ATP-dependent protease; Diffraction Structural Biology; FtsH; Helicobacter pylori
• ISSN: 1600-5775; 0909-0495; 1600-5775
• DOI: 10.1107/S090904950706846X

The ATP‐dependent protease, FtsH, degrades misassembled membrane proteins for quality control like SecY, subunit a of FoF1‐ATPase, and YccA, and digests short‐lived soluble proteins in order to control their cellular regulation, including σ32, LpxC and λcII. The FtsH protein has an N‐terminal transmembrane segment and a large cytosolic region that consists of two domains, an ATPase and a protease domain. To provide a structural basis for the nucleotide‐dependent domain motions and a better understanding of substrate translocation, the crystal structures of the Helicobacter pylori (Hp) FtsH ATPase domain in the nucleotide‐free state and complexed with ADP, were determined. Two different structures of HpFtsH ATPase were observed, with the nucleotide‐free state in an asymmetric unit, and these structures reveal the new forms and show other conformational differences between the nucleotide‐free and ADP‐bound state compared with previous structures. In particular, one HpFtsH Apo structure has a considerable rotation difference compared with the HpFtsH ADP complex, and this large conformational change reveals that FtsH may have the mechanical force needed for substrate translocation.