4S05

Crystal structure of Klebsiella pneumoniae PmrA in complex with PmrA box DNA

4S05 の概要

• エントリーDOI: 10.2210/pdb4s05/pdb
• 関連するPDBエントリー: 4S04
• 分子名称: DNA-binding transcriptional regulator BasR, DNA (26-MER), BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• 機能のキーワード: two-component system, response regulator, pmra, transcription-dna complex, transcription/dna
• 由来する生物種: Klebsiella pneumoniae; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68761.87

構造登録者

Hsiao, C.D.,Weng, T.H.,Li, Y.C. (登録日: 2014-12-30, 公開日: 2015-11-11, 最終更新日: 2024-02-28)

主引用文献

Lou, Y.C.,Weng, T.H.,Li, Y.C.,Kao, Y.F.,Lin, W.F.,Peng, H.L.,Chou, S.H.,Hsiao, C.D.,Chen, C.
Structure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNA.
Nat Commun, 6:8838-8838, 2015

PubMed Abstract: PmrA, an OmpR/PhoB family response regulator, manages genes for antibiotic resistance. Phosphorylation of OmpR/PhoB response regulator induces the formation of a symmetric dimer in the N-terminal receiver domain (REC), promoting two C-terminal DNA-binding domains (DBDs) to recognize promoter DNA to elicit adaptive responses. Recently, determination of the KdpE-DNA complex structure revealed an REC-DBD interface in the upstream protomer that may be necessary for transcription activation. Here, we report the 3.2-Å-resolution crystal structure of the PmrA-DNA complex, which reveals a similar yet different REC-DBD interface. However, NMR studies show that in the DNA-bound state, two domains tumble separately and an REC-DBD interaction is transiently populated in solution. Reporter gene analyses of PmrA variants with altered interface residues suggest that the interface is not crucial for supporting gene expression. We propose that REC-DBD interdomain dynamics and the DBD-DBD interface help PmrA interact with RNA polymerase holoenzyme to activate downstream gene transcription.

PubMed: 26564787
DOI: 10.1038/ncomms9838

実験手法

X-RAY DIFFRACTION (3.8 Å)