凝溶胶蛋白在F-肌动蛋白上结合位点的确定：对切割和封端的影响。
Determination of the gelsolin binding site on F-actin: implications for severing and capping.
作者信息
McGough A, Chiu W, Way M
机构信息
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA.
出版信息
Biophys J. 1998 Feb;74(2 Pt 1):764-72. doi: 10.1016/S0006-3495(98)74001-9.
Abstract
Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes.
摘要
凝溶胶蛋白是一种六结构域蛋白，通过切断、封端和成核细丝来调节肌动蛋白组装。我们利用电子冷冻显微镜和螺旋重建技术来确定其在F-肌动蛋白上的结合位点。为了在切断条件下获得完全修饰的细丝，我们研究了一种与凝溶胶蛋白相比切断效率降低的衍生物（G2-6）。通过电子冷冻显微镜和螺旋重建技术获得了G2-6:F-肌动蛋白的三维重建结构。该结构表明，凝溶胶蛋白结合细丝时会桥接两个纵向相关的单体。G2-6的F-肌动蛋白结合区域轴向位于上部肌动蛋白单体亚结构域3的中心，径向位于亚结构域1和3之间。我们的结果表明，为了发生切断，凝溶胶蛋白和肌动蛋白都会发生大的构象变化。
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本文引用的文献
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