4Q11

Crystal structure of Proteus mirabilis transcriptional regulator protein Crl at 1.95A resolution

4Q11 の概要

• エントリーDOI: 10.2210/pdb4q11/pdb
• 関連するPDBエントリー: 3RPJ
• 分子名称: Sigma factor-binding protein Crl, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total)
• 機能のキーワード: transcription regulator, sigma factor
• 由来する生物種: Proteus mirabilis
• 細胞内の位置: Cytoplasm (By similarity): B4EUU9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31942.82

構造登録者

Norel, F.,Mayer, C.,Saul, F.A.,Haouz, A. (登録日: 2014-04-02, 公開日: 2014-08-06, 最終更新日: 2023-09-20)

主引用文献

Cavaliere, P.,Levi-Acobas, F.,Mayer, C.,Saul, F.A.,England, P.,Weber, P.,Raynal, B.,Monteil, V.,Bellalou, J.,Haouz, A.,Norel, F.
Structural and functional features of Crl proteins and identification of conserved surface residues required for interaction with the RpoS/ sigma S subunit of RNA polymerase.
Biochem.J., 463:215-224, 2014

PubMed Abstract: In many γ-proteobacteria, the RpoS/σS sigma factor associates with the core RNAP (RNA polymerase) to modify global gene transcription in stationary phase and under stress conditions. The small regulatory protein Crl stimulates the association of σS with the core RNAP in Escherichia coli and Salmonella enterica serovar Typhimurium, through direct and specific interaction with σS. The structural determinants of Crl involved in σS binding are unknown. In the present paper we report the X-ray crystal structure of the Proteus mirabilis Crl protein (CrlPM) and a structural model for Salmonella Typhimurium Crl (CrlSTM). Using a combination of in vivo and in vitro assays, we demonstrated that CrlSTM and CrlPM are structurally similar and perform the same biological function. In the Crl structure, a cavity enclosed by flexible arms contains two patches of conserved and exposed residues required for σS binding. Among these, charged residues that are likely to be involved in electrostatic interactions driving Crl-σS complex formation were identified. CrlSTM and CrlPM interact with domain 2 of σS with the same binding properties as with full-length σS. These results suggest that Crl family members share a common mechanism of σS binding in which the flexible arms of Crl might play a dynamic role.

PubMed: 25056110
DOI: 10.1042/BJ20140578

実験手法

X-RAY DIFFRACTION (1.95 Å)