2cea: Difference between revisions

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==Overview==

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.

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 Structure==

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[[Category: metalloprotease]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:44 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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 Structure==
@@ Line 23: / Line 23: @@
 [[Category: metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:34:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:44 2008''