title: Structural studies on Helicobacter pyloriATP-dependent protease, FtsH.
abstract: 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 sigma32, LpxC and lambdacII. 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.
authors.affiliation: Department of Life Science, Cell Dynamics Research Center, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea.
authors.forename: Sung Hyun
authors.initials: SH
authors.lastname: Kim
authors.forename: Gil Bu
authors.initials: GB
authors.lastname: Kang
authors.forename: Hye Eun
authors.initials: HE
authors.lastname: Song
authors.forename: Sang Jin
authors.initials: SJ
authors.lastname: Park
authors.forename: Man Ho
authors.initials: MH
authors.lastname: Bea
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; C102670:FtsH protein, Helicobacter; D008565:Membrane Proteins; D000255:Adenosine Triphosphate