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| [[Image:2cea.gif|left|200px]] | | {{Seed}} |
| | [[Image:2cea.png|left|200px]] |
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| {{STRUCTURE_2cea| PDB=2cea | SCENE= }} | | {{STRUCTURE_2cea| PDB=2cea | SCENE= }} |
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| '''WILDTYPE'''
| | ===WILDTYPE=== |
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| ==Overview==
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| 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 line below this paragraph, {{ABSTRACT_PUBMED_16484367}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16484367 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16484367}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ftsh]] | | [[Category: Ftsh]] |
| [[Category: Metalloprotease]] | | [[Category: Metalloprotease]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:56:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:32:06 2008'' |
