A mutational wrench in the HAMP gearbox. Academic Article

abstract

• 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.

authors

• Manson, Michael

published proceedings

• Mol Microbiol

author list (cited authors)

• Manson, M. D.

citation count

• 3

complete list of authors

• Manson, Michael D

publication date

• September 2009

publisher

• Wiley  Publisher

published in

• Molecular Microbiology  Journal

keywords

• Bacterial Physiological Phenomena
• Bacterial Proteins
• Membrane Proteins
• Models, Biological
• Models, Chemical
• Models, Molecular
• Protein Structure, Secondary
• Protein Structure, Tertiary
• Signal Transduction

PubMed Central ID

• 19678895

Digital Object Identifier (DOI)

• 10.1111/j.1365-2958.2009.06818.x

start page

• 742

end page

• 746

volume

• 73

issue

• 5

URL

• http://dx.doi.org/10.1111/j.1365-2958.2009.06818.x