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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Journal of bacteriology

Structural plasticity and distinct drug-binding modes of LfrR, a mycobacterial efflux pump regulator

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of bacteriology - 09 Oct 2009

Bellinzoni M, Buroni S, Schaeffer F, Riccardi G, De Rossi E, Alzari PM

Link to Pubmed [PMID] – 19820093

J. Bacteriol. 2009 Dec;191(24):7531-7

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.

http://www.ncbi.nlm.nih.gov/pubmed/19820093