Lemmin T Soto CS Clinthorne G DeGrado WF Dal Peraro M 2013 The PhoQP two-component system is a signaling complex essential for bacterial virulence and cationic antimicrobial peptide resistance. PhoQ is the histidine kinase chemoreceptor of this tandem machine and assembles in a homodimer conformation spanning the bacterial inner membrane. Currently, a full understanding of the PhoQ signal transduction is hindered by the lack of a complete atomistic structure. In this study, an atomistic model of the key transmembrane (TM) domain is assembled by using molecular simulations, guided by experimental cross-linking data. The formation of a polar pocket involving Asn202 in the lumen of the tetrameric TM bundle is crucial for the assembly and solvation of the domain. Moreover, a concerted displacement of the TM helices at the periplasmic side is found to modulate a rotation at the cytoplasmic end, supporting the transduction of the chemical signal through a combination of scissoring and rotational movement of the TM helices. application/pdf https://sonar.ch/global/documents/96995 eng info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pcbi.1002878 info:eu-repo/semantics/altIdentifier/pmid/23359663 info:eu-repo/semantics/openAccess PLoS computational biology. - 2013 Escherichia coli Histidine Kinase Membrane Proteins Models, Molecular Molecular Dynamics Simulation Protein Kinases Signal Transduction Assembly of the transmembrane domain of E. coli PhoQ histidine kinase: implications for signal transduction from molecular simulations. http://purl.org/coar/resource_type/c_6501