ArticleThe Journal of biological chemistry2013
Structure and activity of the flagellar rotor protein FliY: a member of the CheC phosphatase family.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Altering chemotaxis as a strategy to enhance the foraging range of motility-restricted bacteria.Communications biology · 2026Article
- First report on in-depth genome and comparative genome analysis of a metal-resistant bacteriumFrontiers in microbiology · 2024Article
- Parallel genetic adaptation ofMicrobial genomics · 2023Article
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- Complete genome of Sphingomonas paucimobilis ZJSH1, an endophytic bacterium from Dendrobium officinale with stress resistance and growth promotion potential.Archives of microbiology · 2023Article
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Specific Features of the Proteomic Response of Thermophilic BacteriumInternational journal of molecular sciences · 2022Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- A Shaving Proteomic Approach to Unveil Surface Proteins Modulation of Multi-Drug ResistantFrontiers in medicine · 2022Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Article
- Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Suppressor mutations in ribosomal proteins and FliY restore Bacillus subtilis swarming motility in the absence of EF-P.PLoS genetics · 2019Article
- One Basic Blueprint, Many Different Motors.Journal of bacteriology · 2019Article
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
- Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system inThe Journal of biological chemistry · 2018Article
- Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Royal Society open science · 2018Article
- Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression inFrontiers in microbiology · 2018Article
- Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C-ring assembly in T3SS.Molecular microbiology · 2016Article
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5 authors.
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Abstract
backgroundFliY is a flagellar rotor protein of the CheC phosphatase family.
resultsThe FliY structure resembles that of the rotor protein FliM but contains two active centers for CheY dephosphorylation.
conclusionFliY incorporates properties of the FliM/FliN rotor proteins and the CheC/CheX phosphatases to serve multiple functions in the flagellar switch. SIGNIFICANCE: FliY distinguishes flagellar architecture and function in different types of bacteria. Rotating flagella propel bacteria toward favorable environments. Sense of rotation is determined by the intracellular response regulator CheY, which when phosphorylated (CheY-P) interacts directly with the flagellar motor. In many different types of bacteria, the CheC/CheX/FliY (CXY) family of phosphatases terminates the CheY-P signal. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. The 2.5 Å resolution crystal structure of the FliY catalytic domain from Thermotoga maritima bears strong resemblance to the middle domain of FliM. Regions of FliM that mediate contacts within the rotor compose the phosphatase active sites in FliY. Despite the similarity between FliY and FliM, FliY does not bind FliG and thus is unlikely to be a substitute for FliM in the center of the switch complex. Solution studies indicate that FliY dimerizes through its C-terminal domains, which resemble the Escherichia coli switch complex component FliN. FliY differs topologically from the E. coli chemotaxis phosphatase CheZ but appears to utilize similar structural motifs for CheY dephosphorylation in close analogy to CheX. Recognition properties and phosphatase activities of site-directed mutants identify two pseudosymmetric active sites in FliY (Glu(35)/Asn(38) and Glu(132)/Asn(135)), with the second site (Glu(132)/Asn(135)) being more active. A putative N-terminal CheY binding domain conserved with FliM is not required for binding CheY-P or phosphatase activity.
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