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使用一种带有十一金标记的鬼笔环肽衍生物评估丝状肌动蛋白的原子模型。

Evaluating atomic models of F-actin with an undecagold-tagged phalloidin derivative.

作者信息

Steinmetz M O, Stoffler D, Müller S A, Jahn W, Wolpensinger B, Goldie K N, Engel A, Faulstich H, Aebi U

机构信息

M.E. Müller Institute for Microscopy, University of Basel, Switzerland.

出版信息

J Mol Biol. 1998 Feb 13;276(1):1-6. doi: 10.1006/jmbi.1997.1529.

Abstract

We have prepared an undecagold-tagged phalloidin derivative to determine this mushroom toxin's binding site and orientation within the F-actin filament by scanning transmission electron microscopy (STEM) and 3-D helical reconstruction. Remarkably, when stoichiometrically bound to F-actin, the undecagold moiety of the derivative could be directly visualized by STEM along the two half-staggered long-pitch helical strands of single filaments. Most importantly, the structural data obtained when combined with various biochemical constraints enabled us to critically evaluate two distinct atomic models of the F-actin filament (i.e. the Holmes-Lorenz versus the Schutt-Lindberg model). Taken together, our data are in excellent agreement with the Holmes-Lorenz model.

摘要

我们制备了一种带有十一金标记的鬼笔环肽衍生物,通过扫描透射电子显微镜(STEM)和三维螺旋重建来确定这种蘑菇毒素在F-肌动蛋白丝中的结合位点和取向。值得注意的是,当以化学计量比与F-肌动蛋白结合时,衍生物的十一金部分可以通过STEM沿着单丝的两条半交错长间距螺旋链直接可视化。最重要的是,结合各种生化约束条件获得的结构数据使我们能够严格评估F-肌动蛋白丝的两种不同原子模型(即霍姆斯-洛伦兹模型与舒特-林德伯格模型)。综合来看,我们的数据与霍姆斯-洛伦兹模型非常吻合。

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