ArticleProceedings of the National Academy of Sciences of the United States of America2004
In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The protein-water H-bond network for bacterial response regulator REC domain activation.Journal of structural biology: X · 2026Article
- Diverse domain architectures of CheA histidine kinase, a central component of bacterial and archaeal chemosensory systems.Microbiology spectrum · 2024Article
- Design of an artificial phage-display library based on a new scaffold improved for average stability of the randomized proteins.Scientific reports · 2023Article
- Computational Methods and Deep Learning for Elucidating Protein Interaction Networks.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Engineered chemotaxis core signaling units indicate a constrained kinase-off state.Science signaling · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Site-Specific Incorporation of a CuThe journal of physical chemistry. B · 2018Article
- Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromThe Journal of biological chemistry · 2017Article
- Programming Post-Translational Control over the Metabolic Labeling of Cellular Proteins with a Noncanonical Amino Acid.ACS synthetic biology · 2017Article
- A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Biochemistry · 2016Article
- 3DIANA: 3D Domain Interaction Analysis: A Toolbox for Quaternary Structure Modeling.Biophysical journal · 2016Article
- Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Journal of molecular biology · 2015Article
- Combining random gene fission and rational gene fusion to discover near-infrared fluorescent protein fragments that report on protein-protein interactions.ACS synthetic biology · 2015Article
- Coevolved Mutations Reveal Distinct Architectures for Two Core Proteins in the Bacterial Flagellar Motor.PloS one · 2015Article
- Article
- On the binding affinity of macromolecular interactions: daring to ask why proteins interact.Journal of the Royal Society, Interface · 2013Review
- Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.Biochemistry · 2012Article
- Alternative protein-protein interfaces are frequent exceptions.PLoS computational biology · 2012Article
- Structural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterparts.International journal of biological macromolecules · 2011Article
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5 authors.
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Abstract
Although interfaces mediating protein-protein interactions are thought to be under strong evolutionary constraints, binding of the chemotaxis histidine kinase CheA to its phosphorylation target CheY suggests otherwise. The structure of Thermotoga maritima CheA domain P2 in complex with CheY reveals a different association than that observed for the same Escherichia coli proteins. Similar regions of CheY bind CheA P2 in the two systems, but the CheA P2 domains differ by an approximately 90 degrees rotation. CheA binds CheY with identical affinity in T. maritima and E. coli at the vastly different temperatures where the respective organisms live. Distinct sets of P2 residues mediate CheY binding in the two complexes; conservation patterns of these residues in CheA and compensations in CheY delineate two families of prokaryotic chemotaxis systems. A protein complex that has the same components and general function in different organisms, but an altered structure, indicates unanticipated complexity in the evolution of protein-protein interactions and cautions against extrapolating structural data from homologs.
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