ArticleProtein science : a publication of the Protein Society2002
Site-directed spin labeling of a bacterial chemoreceptor reveals a dynamic, loosely packed transmembrane domain.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code.Nature communications · 2024Article
- The distal cytoplasmic tail of the influenza A M2 protein dynamically extends from the membrane.Biochimica et biophysica acta. Biomembranes · 2019Article
- Bacterial Chemoreceptor Dynamics: Helical Stability in the Cytoplasmic Domain Varies with Functional Segment and Adaptational Modification.Journal of molecular biology · 2016Article
- Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.Protein science : a publication of the Protein Society · 2015Article
- Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ.Structure (London, England : 1993) · 2014Article
- Influence of membrane lipid composition on a transmembrane bacterial chemoreceptor.The Journal of biological chemistry · 2012Article
- Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity.Protein science : a publication of the Protein Society · 2006Article
- Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE).Journal of biomolecular NMR · 2005Article
- Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues.Protein science : a publication of the Protein Society · 2004Article
- Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR.Biophysical journal · 2004Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
We used site-directed spin labeling and electron paramagnetic resonance spectroscopy to investigate dynamics and helical packing in the four-helix transmembrane domain of the homodimeric bacterial chemoreceptor Trg. We focused on the first transmembrane helix, TM1, particularly on the nine-residue sequence nearest the periplasm, because patterns of disulfide formation between introduced cysteines had identified that segment as the region of closest approach among neighboring transmembrane helices. Along this sequence, mobility and accessibility of the introduced spin label were characteristic of loosely packed or solvent-exposed side chains. This was also the case for eight additional positions around the circumference and along the length of TM1. For the continuous nine-residue sequence near the periplasm, mobility and accessibility varied only modestly as a function of position. We conclude that side chains of TM1 that face the interior of the four-helix domain interact with neighboring helices but dynamic movement results in loose packing. Compared to transmembrane segments of other membrane proteins reconstituted into lipid bilayers and characterized by site-directed spin labeling, TM1 of chemoreceptor Trg is the most dynamic and loosely packed. A dynamic, loosely packed chemoreceptor domain can account for many experimental observations about the transmembrane domains of chemoreceptors.
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