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首页> 外文期刊>Journal of Molecular Biology >pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.
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pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.

机译：pH依赖的相互作用指导折叠和控制β-桶状膜蛋白OmpG的跨膜孔。

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摘要

The physical interactions that switch the functional state of membrane proteins are poorly understood. Previously, the pH-gating conformations of the beta-barrel forming outer membrane protein G (OmpG) from Escherichia coli have been solved. When the pH changes from neutral to acidic the flexible extracellular loop L6 folds into and closes the OmpG pore. Here, we used single-molecule force spectroscopy to structurally localize and quantify the interactions that are associated with the pH-dependent closure. At acidic pH, we detected a pH-dependent interaction at loop L6. This interaction changed the (un)folding of loop L6 and of beta-strands 11 and 12, which connect loop L6. All other interactions detected within OmpG were unaffected by changes in pH. These results provide a quantitative and mechanistic explanation of how pH-dependent interactions change the folding of a peptide loop to gate the transmembrane pore. They further demonstrate how the stability of OmpG is optimized so that pH changes modify only those interactions necessary to gate the transmembrane pore.
机译：切换膜蛋白功能状态的物理相互作用了解甚少。以前，已经解决了来自大肠杆菌的β-桶形成外膜蛋白G（OmpG）的pH门控构象。当pH从中性变为酸性时，柔性细胞外环L6会折叠并封闭OmpG孔。在这里，我们使用单分子力光谱法在结构上定位和量化与pH依赖性封闭相关的相互作用。在酸性pH下，我们在L6环处检测到pH依赖性相互作用。这种相互作用改变了环L6以及连接环L6的β链11和12的（解折叠）。在OmpG中检测到的所有其他相互作用均不受pH值变化的影响。这些结果为pH依赖性相互作用如何改变肽环的折叠以门控跨膜孔提供了定量和机械的解释。他们进一步证明了如何优化OmpG的稳定性，从而使pH值的变化仅修饰门控跨膜孔所必需的相互作用。

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