Dynamic Behavior of Trigger Factor on the Ribosome
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- 作者：J. Deeng1 ; K.Y. Chan2 ; E.O. van der Sluis1 ; O. Berninghausen1 ; W. Han2 ; J. Gumbart3 ; K. Schulten2 ; B. Beatrix1 ; beatrix@genzentrum.lmu.de" class="auth_mail" title="E-mail the corresponding author ; R. Beckmann1 ; beckmann@genzentrum.lmu.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：TF ; trigger factor ; RBD ; ribosome-binding domain ; PPIase ; peptidyl-prolyl cis/trans-isomerase ; MST ; microscale thermophoresis ; MD ; molecular dynamics ; NC ; nascent chain ; cryo-EM ; cryo-electron microscopy ; GatD ; galactitol-1-phosphate dehydrogenase ; RNCs ; ribosome&ndash ; NC complexes ; MDFF ; molecular dynamics flexible fitting ; EM ; electron microscopy ; CG ; coarse-grained ; PACE ; protein in atomistic details coupled with coarse-grained environment ; PCA ; principal component analysis
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：11 September 2016
- 年：2016
- 卷：428
- 期：18
- 页码：3588-3602
- 全文大小：2208 K
文摘
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Trigger factor's interaction with NCs on the ribosome is studied.
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We have analyzed TF–ribosome–NC complexes via cryo-electron microscopy.
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When bound to the ribosome, TF's flexibility depends on the NC length.
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The rearranged RBD of TF provides a first landing platform for the NC.
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Conformational dynamics of TF on the ribosome are coordinated with NC binding.