2CEA

CELL DIVISION PROTEIN FTSH

Summary for 2CEA

• Entry DOI: 10.2210/pdb2cea/pdb
• Related: 2CE7
• Descriptor: CELL DIVISION PROTEIN FTSH, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: cell division, metalloprotease, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 6
• Total formula weight: 319639.97

Authors

Bieniossek, C.,Baumann, U. (deposition date: 2006-02-03, release date: 2006-02-09, Last modification date: 2024-05-08)

Primary citation

Bieniossek, C.,Schalch, T.,Bumann, M.,Meister, M.,Meier, R.,Baumann, U.
The Molecular Architecture of the Metalloprotease Ftsh.
Proc.Natl.Acad.Sci.USA, 103:3066-, 2006

PubMed Abstract: The ATP-dependent integral membrane protease FtsH is universally conserved in bacteria. Orthologs exist in chloroplasts and mitochondria, where in humans the loss of a close FtsH-homolog causes a form of spastic paraplegia. FtsH plays a crucial role in quality control by degrading unneeded or damaged membrane proteins, but it also targets soluble signaling factors like sigma(32) and lambda-CII. We report here the crystal structure of a soluble FtsH construct that is functional in caseinolytic and ATPase assays. The molecular architecture of this hexameric molecule consists of two rings where the protease domains possess an all-helical fold and form a flat hexagon that is covered by a toroid built by the AAA domains. The active site of the protease classifies FtsH as an Asp-zincin, contrary to a previous report. The different symmetries of protease and AAA rings suggest a possible translocation mechanism of the target polypeptide chain into the interior of the molecule where the proteolytic sites are located.

PubMed: 16484367
DOI: 10.1073/PNAS.0600031103

Experimental method

X-RAY DIFFRACTION (2.75 Å)