ArticleMolecular microbiology2014
The HAMP signal-conversion domain: static two-state or dynamic three-state?
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026Article
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024Article
- New Roles for HAMP Domains: the Tri-HAMP Region of Pseudomonas aeruginosa Aer2 Controls Receptor Signaling and Cellular Localization.Journal of bacteriology · 2022Article
- Allosteric mechanism of signal transduction in the two-component system histidine kinase PhoQ.eLife · 2021Article
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Protein design-scapes generated by microfluidic DNA assembly elucidate domain coupling in the bacterial histidine kinase CpxA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis.PLoS pathogens · 2020Article
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function.PloS one · 2018Article
- Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea.Cellular and molecular life sciences : CMLS · 2017Review
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
- Signal transduction in histidine kinases: insights from new structures.Structure (London, England : 1993) · 2015Review
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
- Bacterial chemoreceptors and chemoeffectors.Cellular and molecular life sciences : CMLS · 2015Review
- Identification of functional candidates amongst hypothetical proteins of Treponema pallidum ssp. pallidum.PloS one · 2015Article
- Functional suppression of HAMP domain signaling defects in the E. coli serine chemoreceptor.Journal of molecular biology · 2014Article
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Abstract
The 50-residue HAMP domain converts input signal into output response in a variety of transmembrane signal transduction proteins, including methyl-accepting chemotaxis proteins and histidine kinases. HAMP domains are present in many other contexts as well. Despite focused study over the past decade, the question remains: How does this small domain play such a large role for so many different proteins? Analysis of structural models for the Afl1503 and Aer2 HAMP domains has generated hypotheses in which the HAMP domain assumes either of two discrete forms that generate opposing signal output. In contrast, genetic analysis of the HAMP domain from the Tsr methyl-accepting chemotaxis protein resulted in a distinct hypothesis, the biphasic dynamic bundle. In this hypothesis, signalling involves differential packing stabilities of the HAMP domain four-helix bundle, marked by at least three distinct states. Here I summarize and compare these hypotheses in the context of a deletion analysis that further explores the biphasic dynamic bundle hypothesis.
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