Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
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.

Bibliography

Bieniossek, C., Schalch, T., Bumann, M., Meister, M., Meier, R., & Baumann, U. (2006). The molecular architecture of the metalloprotease FtsH. Proceedings of the National Academy of Sciences, 103(9), 3066–3071.

Authors 6
  1. Christoph Bieniossek (first)
  2. Thomas Schalch (additional)
  3. Mario Bumann (additional)
  4. Markus Meister (additional)
  5. Reto Meier (additional)
  6. Ulrich Baumann (additional)
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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)
Funders 0

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@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} }