SummaryHAMP domains communicate between input and output signalling elements in bacterial proteins. In the Tsr chemoreceptor, they convert axial movement of transmembrane helix 2 into changes in packing of the cytoplasmic kinase‐control module (KCM). Zhou et al. suggest transmembrane helix 2 ‘tugs’ on HAMP to destabilize x‐da packing of the parallel four‐helix bundle of the HAMP homodimer. Attractants would inhibit tugging. HAMP stability may be inversely related to stability of the a‐d packing of the anti‐parallel four‐helix bundle of KCM, a relationship possibly facilitated by HAMP/KCM helical mismatch. The beauty of this idea lies in its simplicity and testability.
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