亚纳米分辨率下的裂殖酵母 26S 蛋白酶体结构。
Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.
机构信息
Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
出版信息
Proc Natl Acad Sci U S A. 2010 Dec 7;107(49):20992-7. doi: 10.1073/pnas.1015530107. Epub 2010 Nov 22.
Abstract
The structure of the 26S proteasome from Schizosaccharomyces pombe has been determined to a resolution of 9.1 Å by cryoelectron microscopy and single particle analysis. In addition, chemical cross-linking in conjunction with mass spectrometry has been used to identify numerous residue pairs in close proximity to each other, providing an array of spatial restraints. Taken together these data clarify the topology of the AAA-ATPase module in the 19S regulatory particle and its spatial relationship to the α-ring of the 20S core particle. Image classification and variance analysis reveal a belt of high "activity" surrounding the AAA-ATPase module which is tentatively assigned to the reversible association of proteasome interacting proteins and the conformational heterogeneity among the particles. An integrated model is presented which sheds light on the early steps of protein degradation by the 26S complex.
摘要
通过冷冻电镜和单颗粒分析，已将来自酿酒酵母的 26S 蛋白酶体的结构解析至 9.1Å 的分辨率。此外，还使用化学交联结合质谱鉴定了许多彼此接近的残基对，提供了一系列的空间约束。这些数据共同阐明了 19S 调节颗粒中的 AAA-ATP 酶模块的拓扑结构及其与 20S 核心颗粒的α环的空间关系。图像分类和方差分析显示，在 AAA-ATP 酶模块周围有一个高“活性”带，该带被暂时分配给蛋白酶体相互作用蛋白的可逆结合以及颗粒之间的构象异质性。提出了一个综合模型，该模型揭示了 26S 复合物进行蛋白质降解的早期步骤。
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