Refutation: Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus.
By I. Monk, T. Seemann, B. Howden, T. Stinear. 2016
106 citations recorded by the source corpus.
In a recent report in Nature Communications, Ji et al., (2016) describe the structure of the extracytoplasmic Per-Arnt-Sim (PAS) domain of WalK (WalKEC-PAS), the sensor kinase of the essential two-component regulator WalKR in Staphylococcus aureus. The authors make two independent walK S. aureus mutants by changing two amino acid residues they postulate from structural analysis and comparisons might be important for signal transduction. We have also been exploring the function of WalKR and were surprised by the striking phenotypic impact of these single amino acid substitutions in the WalK sensor, which are contrary to our own (unpublished) observations.
Subfields: Infectious Diseases, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4769f8256ea8d4af1ab00fcf110412621495a99f
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In Molecular Biology
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