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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 : Bio-protocol

Snapshots of the Signaling Complex DesK:DesR in Different Functional States Using Rational Mutagenesis and X-ray Crystallography.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Bio-protocol - 20 Aug 2017

Imelio JA, Larrieux N, Mechaly AE, Trajtenberg F, Buschiazzo A,

Link to Pubmed [PMID] – 34541173

Link to DOI – 10.21769/BioProtoc.2510

Bio Protoc 2017 Aug; 7(16): e2510

We have developed protocols to generate site-specific variants of the histidine-kinase DesK and its cognate response regulator DesR, conducive to trapping different signaling states of the proteins. Co-expression of both partners in E. coli, ensuring an excess of the regulator, was essential for soluble production of the DesK:DesR complexes and further purification. The 3D structures of the complex trapped in the phosphotransferase and in the phosphatase reaction steps, were solved by X-ray crystallography using molecular replacement. The solution was not trivial, and we found that in silico-generated models used as search probes, were instrumental to succeeding in placing a large portion of the complex in the asymmetric unit. Electron density maps were then clear enough to allow for manual model building attaining complete atomic models. These methods contribute to tackling a major challenge in the bacterial signaling field, namely obtaining stable kinase:regulator complexes, in distinct conformational states, amenable for high-resolution crystallographic studies.

https://pubmed.ncbi.nlm.nih.gov/34541173