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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Journal of structural biology

Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance

Team: Crystallography
Team: Structural Microbiology
Member: Ahmed Haouz
Member: Ariel Mechaly
Member: Pedro Alzari
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of structural biology - 04 Aug 2018

Mechaly AE, Haouz A, Sassoon N, Buschiazzo A, Betton JM, Alzari PM

Link to Pubmed [PMID] – 30086390

J. Struct. Biol. 2018 Nov;204(2):165-171

The transcriptional regulator CpxR mediates an adaptive response to envelope stress, tightly linked to virulence and antibiotics resistance in several Gammaproteobacteria pathogens. In this work, we integrated crystallographic and small-angle X-ray scattering data to gain insights into the structure and conformational plasticity of CpxR from Escherichia coli. CpxR dimerizes through two alternative interaction surfaces. Moreover, widely different CpxR conformations coexist in solution, from compact to fully extended ones. The possible functional implications of these structural features are discussed.