2ce7: Difference between revisions
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
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Revision as of 19:01, 5 November 2007
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EDTA TREATED
OverviewOverview
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.
About this StructureAbout this Structure
2CE7 is a Single protein structure of sequence from Thermotoga maritima with ZN, MG and ADP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
The molecular architecture of the metalloprotease FtsH., Bieniossek C, Schalch T, Bumann M, Meister M, Meier R, Baumann U, Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3066-71. Epub 2006 Feb 16. PMID:16484367
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