4DVD

Crystal structure of the disulphide linked knotted homodimer of Psu

4DVD の概要

• エントリーDOI: 10.2210/pdb4dvd/pdb
• 関連するPDBエントリー: 3RX6
• 分子名称: Polarity suppression protein (1 entity in total)
• 機能のキーワード: all alpha protein, transcription termination inhibitor, rho binding, capsid decoration protein of bacteriophage p4, transcription terminator rho helicase, transcription regulator
• 由来する生物種: Enterobacteria phage P4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21362.97

構造登録者

Banerjee, R.,Nath, S.,Sen, U. (登録日: 2012-02-23, 公開日: 2012-11-21, 最終更新日: 2023-11-08)

主引用文献

Banerjee, R.,Nath, S.,Ranjan, A.,Khamrui, S.,Pani, B.,Sen, R.,Sen, U.
The first structure of polarity suppression protein, Psu from enterobacteria phage P4, reveals a novel fold and a knotted dimer
J.Biol.Chem., 287:44667-44675, 2012

PubMed 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.

PubMed: 23150672
DOI: 10.1074/jbc.M112.423202

実験手法

X-RAY DIFFRACTION (3 Å)