Open AccessStructural studies on Helicobacter pylori ATP‐dependent protease, FtsH
Author(s) -
Kim Sung Hyun,
Kang Gil Bu,
Song HyeEun,
Park Sang Jin,
Bea ManHo,
Eom Soo Hyun
Publication year - 2008
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s090904950706846x
Subject(s) - protease , aaa proteins , atpase , nucleotide , protein subunit , transmembrane domain , biochemistry , transmembrane protein , chemistry , enzyme , biophysics , protein structure , cytosol , conformational change , biology , microbiology and biotechnology , amino acid , gene , receptor
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 Hp FtsH 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 Hp FtsH Apo structure has a considerable rotation difference compared with the Hp FtsH ADP complex, and this large conformational change reveals that FtsH may have the mechanical force needed for substrate translocation.