Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH.
Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH.
复制标题
覆盖蛋白酶活性位点的盖螺旋的构象转变对于 FtsH 的 ATP 依赖性蛋白酶活性至关重要。
DOI：
10.1016/j.febslet.2012.07.069
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发表时间：
2012
期刊：
影响因子：
3.5
通讯作者：
Suno R. et al.
中科院分区：
文献类型：
--
作者：
Miyaji;T.;Sawada;K.;Omote;H.Moriyama Y;Moriyama K;曲 正樹ら;稲嶺翔吾・西村裕一・李 京蘭・松島綾美・野瀬 健・Tommaso Costa・下東康幸;Suno R. et al.
当与ADP结合时，ATP依赖性蛋白酶FtsH亚基采用“开放”或“封闭”构象。在开放状态下，蛋白酶催化位点位于由盖状螺旋覆盖的狭窄空间中。这个空间在闭合形式中消失，因为眼睑螺旋在Gly448处弯曲。在这里，我们用稳定螺旋的各种残基取代Gly448。大多数突变体保持低ATP酶活性，并结合底物蛋白，但失去蛋白酶活性。然而，突变体脯氨酸取代失去了这两个活动。我们的研究表明，盖螺旋的构象转变是必不可少的功能的FtsH。蛋白质相互作用的结构总结：FtsH和FtsH通过分子筛结合（查看相互作用）
When bound to ADP, ATP-dependent protease FtsH subunits adopt either an “open” or “closed” conformation. In the open state, the protease catalytic site is located in a narrow space covered by a lid-like helix. This space disappears in the closed form because the lid helix bends at Gly448. Here, we replaced Gly448 with various residues that stabilize helices. Most mutants retained low ATPase activity and bound to the substrate protein, but lost protease activity. However, a mutant proline substitution lost both activities. Our study shows that the conformational transition of the lid helix is essential for the function of FtsH. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: FtsH and FtsHbind by molecular sieving (View Interaction)