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A mutational wrench in the HAMP gearbox
Author(s) -
Manson Michael D.
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2009.06818.x
Subject(s) - hamp , biology , bundle , helix (gastropod) , helix bundle , transmembrane protein , transmembrane domain , biochemistry , protein structure , ecology , receptor , hepcidin , materials science , snail , immunology , composite material , inflammation
Summary HAMP 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.