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Reconstruction of the chemotaxis receptor–kinase assembly

Nature Structural & Molecular Biology volume 13, pages 400–407 (2006)Cite this article

Abstract

In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion–coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA–CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with residues important for receptor interactions and sized to clamp one receptor dimer. CheW residues involved in kinase activation map to interfaces that orient the CheW clamps. CheA regulatory domains associate in crystals through conserved hydrophobic surfaces. Such CheA self-contacts align the CheW receptor clamps for binding receptor tips. Linking layers of ternary complexes with close-packed receptors generates a lattice with reasonable component ratios, cooperative interactions among receptors and accessible sites for modification enzymes.

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Figure 1: Structures of the cytoplasmic domains from T. maritima MCP1143C and E. coli TsrC.
Figure 2: Pulsed ESR for reconstructing protein-protein complexes.
Figure 3: CheW-CheA interactions.
Figure 4: Structural implications for the CheA–CheW–MCP1143C complex.

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Acknowledgements

We thank C. Arango for help with distance-geometry calculations, C. Kim for advice on crystal growth, S. Oga and W. Hubbell for advice on nitroxide spin-labeling, J.S. Parkinson, R. Alexander, I.B. Zhulin and J.J. Falke for helpful discussions and NSLS, CHESS and NE-CAT at the Advanced Photon Source for access to data-collection facilities. This work was supported by US National Institutes of Health grants GM:R01066775 (to B.R.C.) and NCRR:P41-RR016292 (to J.H.F.).

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  1. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, 14853, New York, USA

    Sang-Youn Park, Peter P Borbat, Gabriela Gonzalez-Bonet, Jaya Bhatnagar, Abiola M Pollard, Jack H Freed, Alexandrine M Bilwes & Brian R Crane

  2. The Advanced ESR Technology Center, Cornell University, Ithaca, 14853, New York, USA

    Peter P Borbat & Jack H Freed

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Supplementary information

Supplementary Fig. 1

Initial electron density map for the MCP1143c crystal structure (PDF 1026 kb)

Supplementary Fig. 2

Omit electron density map for the CheAΔ354–CheW crystal structure (PDF 941 kb)

Supplementary Fig. 3

P4 domain orientations in the CheAΔ354–CheW crystallographic complex (PDF 579 kb)

Supplementary Fig. 4

The CheA–CheW–MCP array (PDF 424 kb)

Supplementary Methods (PDF 97 kb)

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Park, SY., Borbat, P., Gonzalez-Bonet, G. et al. Reconstruction of the chemotaxis receptor–kinase assembly. Nat Struct Mol Biol 13, 400–407 (2006). https://doi.org/10.1038/nsmb1085

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