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Asparagine repeat function in a Plasmodium falciparum protein assessed via a regulatable fluorescent affinity tag.通过可调控荧光亲和标签评估恶性疟原虫蛋白中的天冬酰胺重复功能。
Proc Natl Acad Sci U S A. 2011 Mar 15;108(11):4411-6. doi: 10.1073/pnas.1018449108. Epub 2011 Feb 28.
2
Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.亚纳米分辨率下的裂殖酵母 26S 蛋白酶体结构。
Proc Natl Acad Sci U S A. 2010 Dec 7;107(49):20992-7. doi: 10.1073/pnas.1015530107. Epub 2010 Nov 22.
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ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation.ATP 依赖的泛素缀合物与 26S 蛋白酶体结合的步骤，这些步骤决定了降解的命运。
Mol Cell. 2010 Nov 24;40(4):671-81. doi: 10.1016/j.molcel.2010.11.002.
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Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.细胞质和内质网中的蛋白质质量控制：同仇敌忾的兄弟。
Mol Cell. 2010 Oct 22;40(2):238-52. doi: 10.1016/j.molcel.2010.10.001.
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Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae.解析酵母酿酒酵母蛋白酶体盖组装途径。
Biochem Biophys Res Commun. 2010 Jun 11;396(4):1048-53. doi: 10.1016/j.bbrc.2010.05.061. Epub 2010 May 21.
6
Toward an integrated structural model of the 26S proteasome.朝向 26S 蛋白酶体的整合结构模型。
Mol Cell Proteomics. 2010 Aug;9(8):1666-77. doi: 10.1074/mcp.R000002-MCP201. Epub 2010 May 13.
7
An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.26S蛋白酶体的一种原子模型AAA-ATP酶/20S核心颗粒亚复合体。
Biochem Biophys Res Commun. 2009 Oct 16;388(2):228-33. doi: 10.1016/j.bbrc.2009.07.145. Epub 2009 Aug 3.
8
Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.嗜热栖热菌蛋白酶体调节颗粒的结构洞察
Mol Cell. 2009 May 14;34(4):473-84. doi: 10.1016/j.molcel.2009.04.021.
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Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases.蛋白酶体ATP酶中N端底物识别结构域的结构与活性
Mol Cell. 2009 Jun 12;34(5):580-90. doi: 10.1016/j.molcel.2009.04.030. Epub 2009 May 28.
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The proteasome: overview of structure and functions.蛋白酶体：结构与功能概述
Proc Jpn Acad Ser B Phys Biol Sci. 2009;85(1):12-36. doi: 10.2183/pjab.85.12.

蛋白酶体亚基 Rpn6 是一种分子夹具，将核心和调节亚基复合物固定在一起。

The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.

机构信息

Department of Molecular Structural Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.

出版信息

Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):149-54. doi: 10.1073/pnas.1117648108. Epub 2011 Dec 20.

DOI:10.1073/pnas.1117648108
PMID:22187461
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3252951/
Abstract

Proteasomes execute the degradation of most cellular proteins. Although the 20S core particle (CP) has been studied in great detail, the structure of the 19S regulatory particle (RP), which prepares ubiquitylated substrates for degradation, has remained elusive. Here, we report the crystal structure of one of the RP subunits, Rpn6, and we describe its integration into the cryo-EM density map of the 26S holocomplex at 9.1 Å resolution. Rpn6 consists of an α-solenoid-like fold and a proteasome COP9/signalosome eIF3 (PCI) module in a right-handed suprahelical configuration. Highly conserved surface areas of Rpn6 interact with the conserved surfaces of the Pre8 (alpha2) and Rpt6 subunits from the alpha and ATPase rings, respectively. The structure suggests that Rpn6 has a pivotal role in stabilizing the otherwise weak interaction between the CP and the RP.

摘要

蛋白酶体执行大多数细胞蛋白质的降解。尽管 20S 核心颗粒 (CP) 已经被详细研究，但准备进行降解的泛素化底物的 19S 调节颗粒 (RP) 的结构仍然难以捉摸。在这里，我们报告了 RP 亚基之一 Rpn6 的晶体结构，并描述了它如何整合到 26S 完整复合物的 cryo-EM 密度图中，分辨率为 9.1 Å。Rpn6 由一个 α-螺线管样折叠和蛋白酶体 COP9/signalosome eIF3 (PCI) 模块以右手超螺旋构象组成。Rpn6 的高度保守表面区域与 Pre8（α2）和 Rpt6 亚基的保守表面相互作用，分别来自 α 和 ATPase 环。该结构表明，Rpn6 在稳定 CP 和 RP 之间本来较弱的相互作用方面发挥着关键作用。