Hydrophobically stabilized open state for the lateral gate of the Sec translocon
Hydrophobically stabilized open state for the lateral gate of the Sec translocon
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Sec 易位子侧门的疏水稳定打开状态
DOI：
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发表时间：
2010
影响因子：
11.1
通讯作者：
T. F. Miller
中科院分区：
文献类型：
--
作者：
Bin Zhang;T. F. Miller
SEC转运子是蛋白质转运和膜整合的细胞通路的中心组成部分。利用原子论和粗粒度分子模拟，我们研究了转运子的构象图景，并探索了多肽底物在调节转位和整合途径中的作用。在转位子中加入疏水性多肽底物可以稳定侧门的打开以实现膜整合，而亲水性多肽底物有利于关闭的侧门构象。插头部分和多肽底物在转位通道内的相对取向类似地取决于底物是疏水的还是亲水的，而在多肽底物存在的情况下转位子侧向门打开的能量学由多肽与膜的界面能量学决定。讨论了这些结果对调节SEC介导的蛋白质转位与膜整合途径的影响。
The Sec translocon is a central component of cellular pathways for protein translocation and membrane integration. Using both atomistic and coarse-grained molecular simulations, we investigate the conformational landscape of the translocon and explore the role of peptide substrates in the regulation of the translocation and integration pathways. Inclusion of a hydrophobic peptide substrate in the translocon stabilizes the opening of the lateral gate for membrane integration, whereas a hydrophilic peptide substrate favors the closed lateral gate conformation. The relative orientation of the plug moiety and a peptide substrate within the translocon channel is similarly dependent on whether the substrate is hydrophobic or hydrophilic in character, and the energetics of the translocon lateral gate opening in the presence of a peptide substrate is governed by the energetics of the peptide interface with the membrane. Implications of these results for the regulation of Sec-mediated pathways for protein translocation vs. membrane integration are discussed.
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影响因子：
3.3
作者：
Shih, AY;Arkhipov, A;Schulten, K
通讯作者：
Schulten, K
影响因子：
16
作者：
Li, Weikai;Schulman, Sol;Rapoport, Tom A.
通讯作者：
Rapoport, Tom A.
影响因子：
3.4
作者：
Arkhipov, Anton;Yin, Ying;Schulten, Klaus
通讯作者：
Schulten, Klaus
影响因子：
2.9
作者：
Gumbart, James;Schulten, Klaus
通讯作者：
Schulten, Klaus