2cea
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WILDTYPE
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 ... [(full description)]
About this StructureAbout this Structure
2CEA 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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