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The molecular architecture of the metalloprotease FtsH.

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  • 2006-02-18
Published in:
  • Proceedings of the National Academy of Sciences of the United States of America. - 2006
Adenosine Triphosphatases
Aspartic Acid
Bacterial Proteins
Cell Membrane
Crystallography, X-Ray
Membrane Proteins
Metalloproteases
Models, Molecular
Protein Structure, Quaternary
Protein Structure, Tertiary
Substrate Specificity
Thermotoga maritima
English 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.
Language
  • English
Open access status
bronze
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https://sonar.ch/global/documents/172421
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