ArticleJournal of bacteriology2011
Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- Sensing the Reducing Power to Determine the Cell Fate: Flavin Redox-Switches in Signal Transduction.Current microbiology · 2025Review
- The structural logic of dynamic signaling in the Escherichia coli serine chemoreceptor.Protein science : a publication of the Protein Society · 2024Article
- The Structural Logic of Dynamic Signaling in thebioRxiv : the preprint server for biology · 2024Article
- AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024Article
- The type IV pilin PilA couples surface attachment and cell-cycle initiation inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The involvement of McpB chemoreceptor from Pseudomonas aeruginosa PAO1 in virulence.Scientific reports · 2019Article
- 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
- Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer.Molecular microbiology · 2016Article
- Article
- 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
- HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptor.Molecular microbiology · 2014Article
- Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.Journal of molecular biology · 2013Article
- The HAMP signal relay domain adopts multiple conformational states through collective piston and tilt motions.PLoS computational biology · 2013Article
- Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains.PLoS biology · 2013Article
- Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB.Structure (London, England : 1993) · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
HAMP domains are sensory transduction modules that connect input and output domains in diverse signaling proteins from archaea, bacteria, and lower eukaryotes. Here, we employed in vivo disulfide cross-linking to explore the structure of the HAMP domain in the Escherichia coli aerotaxis receptor Aer. Using an Aer HAMP model based on the structure of Archaeoglobus fulgidus Af1503-HAMP, the closest residue pairs at the interface of the HAMP AS-1 and AS-2' helices were determined and then replaced with cysteines and cross-linked in vivo. Except for a unique discontinuity in AS-2, the data suggest that the Aer HAMP domain forms a parallel four-helix bundle that is similar to the structure of Af1503. The HAMP discontinuity was associated with a segment of AS-2 that was recently shown to interact with the Aer-PAS sensing domain. The four-helix HAMP bundle and its discontinuity were maintained in both the kinase-on and kinase-off states of Aer, although differences in the rates of disulfide formation also indicated the existence of different HAMP conformations in the kinase-on and kinase-off states. In particular, the kinase-on state was accompanied by significantly increased disulfide formation rates at the distal end of the HAMP four-helix bundle. This indicates that HAMP signaling may be associated with a tilting of the AS-1 and AS-2' helices, which may be the signal that is transmitted to the kinase control region of Aer.
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