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 σ 32 and λ-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.
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Dates
Type | When |
---|---|
Created | 19 years, 6 months ago (Feb. 16, 2006, 8:43 p.m.) |
Deposited | 3 years, 2 months ago (June 7, 2022, 2:18 a.m.) |
Indexed | 1 month ago (July 24, 2025, 7:48 a.m.) |
Issued | 19 years, 6 months ago (Feb. 16, 2006) |
Published | 19 years, 6 months ago (Feb. 16, 2006) |
Published Online | 19 years, 6 months ago (Feb. 16, 2006) |
Published Print | 19 years, 6 months ago (Feb. 28, 2006) |
@article{Bieniossek_2006, title={The molecular architecture of the metalloprotease FtsH}, volume={103}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0600031103}, DOI={10.1073/pnas.0600031103}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Bieniossek, Christoph and Schalch, Thomas and Bumann, Mario and Meister, Markus and Meier, Reto and Baumann, Ulrich}, year={2006}, month=feb, pages={3066–3071} }