2DI4

Crystal structure of the FtsH protease domain

Summary for 2DI4

• Entry DOI: 10.2210/pdb2di4/pdb
• Descriptor: Cell division protein ftsH homolog, MERCURY (II) ION (3 entities in total)
• Functional Keywords: metalloproteinase, hexamer-ring, hydrolase
• Biological source: Aquifex aeolicus
• Cellular location: Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side: O67077
• Total number of polymer chains: 2
• Total formula weight: 54333.37

Authors

Suno, R.,Niwa, H.,Tsuchiya, D.,Zhang, X.,Yoshida, M.,Morikawa, K. (deposition date: 2006-03-28, release date: 2006-06-27, Last modification date: 2024-11-20)

Primary citation

Suno, R.,Niwa, H.,Tsuchiya, D.,Zhang, X.,Yoshida, M.,Morikawa, K.
Structure of the Whole Cytosolic Region of ATP-Dependent Protease FtsH
Mol.Cell, 22:575-585, 2006

PubMed Abstract: An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.

PubMed: 16762831
DOI: 10.1016/j.molcel.2006.04.020

Experimental method

X-RAY DIFFRACTION (2.79 Å)