PDBsum entry 2r65

Hydrolase

PDB id: 2r65

Contents

Protein chains

249 a.a.

Ligands

ADP ×5

References listed in PDB file

Key reference

• Title: Structural studies on helicobacter pyloriatp-Dependent protease, Ftsh.
• Authors: S.H.Kim, G.B.Kang, H.E.Song, S.J.Park, M.H.Bea, S.H.Eom.
• Ref.: J Synchrotron Radiat, 2008, 15, 208-210. [DOI no: 10.1107/S090904950706846X]
• PubMed id: 18421140

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.