2ce7: Difference between revisions

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.

2CE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ZN, MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CE7 OCA].  

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