1US6

Crystal structure of the quorum-sensing protein TraM from Agrobacterium tumefaciens at 1.65 Ang. resolution

1US6 の概要

• エントリーDOI: 10.2210/pdb1us6/pdb
• 関連するPDBエントリー: 1UPG
• 分子名称: TRANSCRIPTIONAL REPRESSOR TRAM (2 entities in total)
• 機能のキーワード: transcription repressor, negative regulator, quorum-sensing, conjugation, transcripti regulation, repressor, plasmid.
• 由来する生物種: AGROBACTERIUM TUMEFACIENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22830.41

構造登録者

Vannini, A.,Di Marco, S. (登録日: 2003-11-18, 公開日: 2004-05-25, 最終更新日: 2024-05-08)

主引用文献

Vannini, A.,Volpari, C.,Di Marco, S.
Crystal Structure of the Quorum-Sensing Protein Tram and its Interaction with the Transcriptional Regulator Trar
J.Biol.Chem., 279:24291-, 2004

PubMed Abstract: Transfer of the tumor-inducing plasmid in Agrobacterium tumefaciens is controlled by a quorum-sensing system whose main components are the transcriptional regulator TraR and its autoinducer. This system allows bacteria to synchronize infection of the host plant when a "quorum" of cells has been reached. TraM is an A. tumefaciens protein involved in the regulation of this system because it binds to TraR and prevents it from binding DNA. As a first step to understanding the molecular basis for the regulation of TraR by TraM, we have determined the crystal structure of TraM at 1.65 A resolution. This protein is packed as a dimer, with each monomer consisting mainly of two antiparallel alpha helices. Monomers are tightly associated, with a large hydrophobic area buried upon dimerization. Secondly, we characterized the TraR-TraM complex in vitro. TraM (11.4 kDa, monomer molecular mass) binds tightly TraR (27 kDa, monomer molecular mass) forming a stable oligomeric complex that likely accounts for two TraR and two TraM dimers.

PubMed: 15044488
DOI: 10.1074/JBC.M401855200

実験手法

X-RAY DIFFRACTION (1.65 Å)