2V57

Crystal structure of the TetR-like transcriptional regulator LfrR from Mycobacterium smegmatis in complex with proflavine

2V57 の概要

• エントリーDOI: 10.2210/pdb2v57/pdb
• 関連するPDBエントリー: 2WGB
• 分子名称: TETR FAMILY TRANSCRIPTIONAL REPRESSOR LFRR, PROFLAVIN, ISOPROPYL ALCOHOL, ... (5 entities in total)
• 機能のキーワード: tetr, lfrr, repressor, dna-binding, transcription, transcription regulation
• 由来する生物種: MYCOBACTERIUM SMEGMATIS
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 83912.95

構造登録者

Bellinzoni, M.,Buroni, S.,Riccardi, G.,De Rossi, E.,Alzari, P.M. (登録日: 2008-10-02, 公開日: 2009-10-20, 最終更新日: 2024-05-08)

主引用文献

Bellinzoni, M.,Buroni, S.,Schaeffer, F.,Riccardi, G.,De Rossi, E.,Alzari, P.M.
Structural Plasticity and Distinct Drug-Binding Modes of Lfrr, a Mycobacterial Efflux Pump Regulator.
J.Bacteriol., 191:7531-, 2009

PubMed Abstract: The TetR-like transcriptional repressor LfrR controls the expression of the gene encoding the Mycobacterium smegmatis efflux pump LfrA, which actively extrudes fluoroquinolones, cationic dyes, and anthracyclines from the cell and promotes intrinsic antibiotic resistance. The crystal structure of the apoprotein form of the repressor reveals a structurally asymmetric homodimer exhibiting local unfolding and a blocked drug-binding site, emphasizing the significant conformational plasticity of the protein necessary for DNA and multidrug recognition. Crystallographic and calorimetric studies of LfrR-drug complexes further confirm the intrinsic flexibility of the homodimer, which provides a dynamic mechanism to broaden multidrug binding specificity and may be a general property of transcriptional repressors regulating microbial efflux pump expression.

PubMed: 19820093
DOI: 10.1128/JB.00631-09

実験手法

X-RAY DIFFRACTION (1.9 Å)