2R65

Crystal structure of Helicobacter pylori ATP dependent protease, FtsH ADP complex

Summary for 2R65

• Entry DOI: 10.2210/pdb2r65/pdb
• Related: 2R62
• Descriptor: Cell division protease ftsH homolog, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: ftsh, adp, atpase domain, helicobacter pylori, atp-binding, cell cycle, cell division, hydrolase, membrane, metal-binding, metalloprotease, nucleotide-binding, protease, transmembrane
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Cellular location: Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side (Probable): P71408
• Total number of polymer chains: 5
• Total formula weight: 147682.61

Authors

Kim, S.H.,Kang, G.B.,Song, H.-E.,Park, S.J.,Bae, M.-H.,Eom, S.H. (deposition date: 2007-09-05, release date: 2008-09-09, Last modification date: 2023-10-25)

Primary citation

Kim, S.H.,Kang, G.B.,Song, H.-E.,Park, S.J.,Bea, M.-H.,Eom, S.H.
Structural studies on Helicobacter pyloriATP-dependent protease, FtsH
J.SYNCHROTRON RADIAT., 15:208-210, 2008

PubMed 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.

PubMed: 18421140
DOI: 10.1107/S090904950706846X

Experimental method

X-RAY DIFFRACTION (3.3 Å)