The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Ã… resolution
The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Ã… resolution
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DOI：
10.1016/s0969-2126(02)00806-7
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发表时间：
2002-08-01
期刊：
影响因子：
5.7
通讯作者：
Wilkinson, AJ
中科院分区：
文献类型：
--
作者：
Krzywda, S;Brzozowski, AM;Wilkinson, AJ
真细菌和真核细胞器具有膜结合的 ATP 依赖性蛋白酶，可降解错误组装的膜蛋白复合物，并在膜质量控制中发挥重要作用。细菌蛋白酶 FtsH 还降解细胞质调节蛋白的一个有趣子集，包括 sigma(32)、LpxC 和 lambda CII FtsH ATP 酶模块的晶体结构已得到解决，揭示了连接到四螺旋束的 α/β 核苷酸结合结构域，类似于 DNA 中涉及的蛋白质的 AAA 模块 复制和膜融合。 ATP 结合袋中的硫酸根阴离子模拟腺嘌呤核苷酸的 P-磷酸基团。 FtsH 的六聚体形式已经被建模，为核苷酸结合和亚基间催化的可能模式提供了见解。
Eubacteria and eukaryotic cellular organelles have membrane-bound ATP-dependent proteases, which degrade misassembled membrane protein complexes and play a vital role in membrane quality control. The bacterial protease FtsH also degrades an interesting subset of cytoplasmic regulatory proteins, including sigma(32), LpxC, and lambda CII The crystal structure of the ATPase module of FtsH has been solved, revealing an alpha/beta nucleotide binding domain connected to a four-helix bundle, similar to the AAA modules of proteins involved in DNA replication and membrane fusion. A sulfate anion in the ATP binding pocket mimics the P-phosphate group of an adenine nucleotide. A hexamer form of FtsH has been modeled, providing insights into possible modes of nucleotide binding and intersubunit catalysis.