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Crystal structure of activated CheY1 from Helicobacter pylori.

Lam KH, Ling TK, Au SW
J Bacteriol 192 2324-34 (2010)
Related entries: 3h1e, 3h1f, 3h1g

Cited: 17 times
EuropePMC logo PMID: 20207758

Abstract

Chemotaxis is an important virulence factor for Helicobacter pylori colonization and infection. The chemotactic system of H. pylori is marked by the presence of multiple response regulators: CheY1, one CheY-like-containing CheA protein (CheAY2), and three CheV proteins. Recent studies have demonstrated that these molecules play unique roles in the chemotactic signal transduction mechanisms of H. pylori. Here we report the crystal structures of BeF(3(-)-activated CheY1 from H. pylori resolved to 2.4 A. Structural comparison of CheY1 with active-site residues of BeF3(-)-bound CheY from Escherichia coli and fluorescence quenching experiments revealed the importance of Thr84 in the phosphotransfer reaction. Complementation assays using various nonchemotactic E. coli mutants and pull-down experiments demonstrated that CheY1 displays differential association with the flagellar motor in E. coli. The structural rearrangement of helix 5 and the C-terminal loop in CheY1 provide a different interaction surface for FliM. On the other hand, interaction of the CheA-P2 domain with CheY1, but not with CheY2/CheV proteins, underlines the preferential recognition of CheY1 by CheA in the phosphotransfer reaction. Our results provide the first structural insight into the features of the H. pylori chemotactic system as a model for Epsilonproteobacteria.

Articles - 3gwg mentioned but not cited (3)

  1. Crystal structure of activated CheY1 from Helicobacter pylori. Lam KH, Ling TK, Au SW. J Bacteriol 192 2324-2334 (2010)
  2. Conformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio cholerae. Biswas M, Dey S, Khamrui S, Sen U, Dasgupta J. PLoS One 8 e73923 (2013)
  3. Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases. Immormino RM, Starbird CA, Silversmith RE, Bourret RB. Biochemistry 54 3514-3527 (2015)


Reviews citing this publication (5)

  1. Motility and chemotaxis in Campylobacter and Helicobacter . Lertsethtakarn P, Ottemann KM, Hendrixson DR. Annu Rev Microbiol 65 389-410 (2011)
  2. Colonization, localization, and inflammation: the roles of H. pylori chemotaxis in vivo. Johnson KS, Ottemann KM. Curr Opin Microbiol 41 51-57 (2018)
  3. Focus on phosphoaspartate and phosphoglutamate. Attwood PV, Besant PG, Piggott MJ. Amino Acids 40 1035-1051 (2011)
  4. Structural and functional aspects of the Helicobacter pylori secretome. Zanotti G, Cendron L. World J Gastroenterol 20 1402-1423 (2014)
  5. Progress and Potential of Electron Cryotomography as Illustrated by Its Application to Bacterial Chemoreceptor Arrays. Briegel A, Jensen G. Annu Rev Biophys 46 1-21 (2017)

Articles citing this publication (9)

  1. Migration of chemotactic bacteria in soft agar: role of gel concentration. Croze OA, Ferguson GP, Cates ME, Poon WC. Biophys J 101 525-534 (2011)
  2. Structural basis of FliG-FliM interaction in Helicobacter pylori. Lam KH, Lam WW, Wong JY, Chan LC, Kotaka M, Ling TK, Jin DY, Ottemann KM, Au SW. Mol Microbiol 88 798-812 (2013)
  3. A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori. Zhang H, Lam KH, Lam WWL, Wong SYY, Chan VSF, Au SWN. Mol Microbiol 106 690-703 (2017)
  4. Asymmetric random walks reveal that the chemotaxis network modulates flagellar rotational bias in Helicobacter pylori. Antani JD, Sumali AX, Lele TP, Lele PP. Elife 10 e63936 (2021)
  5. The evolutionary path of chemosensory and flagellar macromolecular machines in Campylobacterota. Mo R, Zhu S, Chen Y, Li Y, Liu Y, Gao B. PLoS Genet 18 e1010316 (2022)
  6. Molecular dynamics investigation of Helicobacter pylori chemotactic protein CheY1 and two mutants. Yildirim A, Tekpinar M, Wassenaar TA. J Mol Model 20 2212 (2014)
  7. Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator. Foster CA, Silversmith RE, Immormino RM, Vass LR, Kennedy EN, Pazy Y, Collins EJ, Bourret RB. Biochemistry 60 2130-2151 (2021)
  8. The Divergent Key Residues of Two Agrobacterium fabrum (tumefaciens) CheY Paralogs Play a Key Role in Distinguishing Their Functions. Gao D, Zong R, Huang Z, Ye J, Wang H, Xu N, Guo M. Microorganisms 9 1134 (2021)
  9. Apparent instability of crystallographic refinement in the presence of disordered model fragments and upon insufficiently restrained model geometry. Pozharski E. Acta Crystallogr D Biol Crystallogr 67 966-972 (2011)


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