2CEA
CELL DIVISION PROTEIN FTSH
2CEA の概要
| エントリーDOI | 10.2210/pdb2cea/pdb |
| 関連するPDBエントリー | 2CE7 |
| 分子名称 | CELL DIVISION PROTEIN FTSH, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| 機能のキーワード | cell division, metalloprotease, hydrolase |
| 由来する生物種 | Thermotoga maritima |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 319639.97 |
| 構造登録者 | |
| 主引用文献 | Bieniossek, C.,Schalch, T.,Bumann, M.,Meister, M.,Meier, R.,Baumann, U. The Molecular Architecture of the Metalloprotease Ftsh. Proc.Natl.Acad.Sci.USA, 103:3066-, 2006 Cited by PubMed Abstract: 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. PubMed: 16484367DOI: 10.1073/PNAS.0600031103 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.75 Å) |
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