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Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):271-81. doi: 10.1107/S0907444910048675. Epub 2011 Mar 18.
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Structure and folding of a designed knotted protein.设计的打结蛋白的结构和折叠。
Proc Natl Acad Sci U S A. 2010 Nov 30;107(48):20732-7. doi: 10.1073/pnas.1007602107. Epub 2010 Nov 10.
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Dali server: conservation mapping in 3D.大理服务器：三维保护图谱构建。
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9. doi: 10.1093/nar/gkq366. Epub 2010 May 10.
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PHENIX: a comprehensive Python-based system for macromolecular structure solution.PHENIX：一个基于Python的用于大分子结构解析的综合系统。
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Phaser crystallographic software.相位结晶学软件。
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Interaction surface of bacteriophage P4 protein Psu required for complex formation with the transcription terminator Rho.噬菌体P4蛋白Psu与转录终止因子Rho形成复合物所需的相互作用表面。
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Structural basis for converting a general transcription factor into an operon-specific virulence regulator.将一般转录因子转变为操纵子特异性毒力调节因子的结构基础。
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极性抑制蛋白 Psu 的第一个结构来自于肠杆菌噬菌体 P4，揭示了一种新颖的折叠和打结的二聚体。

The first structure of polarity suppression protein, Psu from enterobacteria phage P4, reveals a novel fold and a knotted dimer.

机构信息

Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF, Bidhannagar, Kolkata 700064, India.

出版信息

J Biol Chem. 2012 Dec 28;287(53):44667-75. doi: 10.1074/jbc.M112.423202. Epub 2012 Nov 12.

DOI:10.1074/jbc.M112.423202
PMID:23150672
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3531781/
Abstract

Psu is a capsid decoration protein of bacteriophage P4 and acts as an antiterminator of Rho-dependent transcription termination in bacteria. So far, no structures have been reported for the Psu protein or its homologues. Here, we report the first structure of Psu solved by the Hg(2+) single wavelength anomalous dispersion method, which reveals that Psu exists as a knotted homodimer and is first of its kind in nature. Each monomer of Psu attains a novel fold around a tight coiled-coil motif. CD spectroscopy and the structure of an engineered disulfide-bridged Psu derivative reveal that the protein folds reversibly and reassembles by itself into the knotted dimeric conformation without the requirement of any chaperone. This structure would help to explain the functional properties of the protein and can be used as a template to design a minimal peptide fragment that can be used as a drug against Rho-dependent transcription termination in bacteria.

摘要

Psu 是噬菌体 P4 的衣壳装饰蛋白，在细菌中充当 Rho 依赖型转录终止的反终止子。到目前为止，还没有报道过 Psu 蛋白或其同源物的结构。在这里，我们通过汞（2+）单波长反常散射方法首次解析了 Psu 的结构，结果表明 Psu 以扭结同源二聚体的形式存在，在自然界中尚属首例。Psu 的每个单体都围绕一个紧密的螺旋-螺旋基序形成一种新颖的折叠。圆二色性（CD）光谱和工程化的二硫键桥连 Psu 衍生物的结构表明，该蛋白可以可逆折叠，并自行重新组装成扭结二聚体构象，而不需要任何伴侣蛋白。该结构有助于解释该蛋白的功能特性，并可作为模板来设计最小肽片段，用作针对细菌中 Rho 依赖型转录终止的药物。