2DS5
Structure of the ZBD in the orthorhomibic crystal from
2DS5 の概要
エントリーDOI | 10.2210/pdb2ds5/pdb |
関連するPDBエントリー | 2DS6 2DS7 2DS8 |
分子名称 | ATP-dependent Clp protease ATP-binding subunit clpX, ZINC ION, CALCIUM ION, ... (5 entities in total) |
機能のキーワード | treble cleft zinc finger, metal binding protein, protein binding |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 11882.38 |
構造登録者 | |
主引用文献 | Park, E.Y.,Lee, B.G.,Hong, S.B.,Kim, H.W.,Jeon, H.,Song, H.K. Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX. J.Mol.Biol., 367:514-526, 2007 Cited by PubMed Abstract: The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial cytosol is carried out by the ClpXP protease and is markedly stimulated by the SspB adaptor protein. It has previously been reported that the amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex formation with the SspB-tail (XB: ClpX-binding motif). In an effort to better understand the recognition of SspB by ClpX and the mechanism of delivery of ssrA-tagged substrates to ClpXP, we have determined the structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each different crystal form and also in complex with XB peptide at 1.6 A resolution. The XB peptide forms an antiparallel beta-sheet with two beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex between ZBD and XB, suggesting that there are two independent SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex structure, in combination with biochemical analyses, can account for key determinants in the recognition of the SspB-tail by ClpX and sheds light on the mechanism of delivery of target proteins to the prokaryotic degradation machine. PubMed: 17258768DOI: 10.1016/j.jmb.2007.01.003 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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