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Comment
. 2007 Feb 20;104(8):2559-60.
doi: 10.1073/pnas.0700278104. Epub 2007 Feb 14.

Ancient chemoreceptors retain their flexibility

John S Parkinson  1
Affiliations
Comment

Ancient chemoreceptors retain their flexibility

John S Parkinson. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Structure and function of MCP molecules. (A) Schematic of an MCP homodimer; individual subunits are not distinguished. P, periplasmic space; CM, cytoplasmic membrane; C, cytoplasm. (B) Schematic of the MCP cytoplasmic domain showing the helical segments in the adaptation and signaling subdomains and the flexible bundle. The thickness of the helices is roughly proportional to their coiled-coil stabilities. Black circles denote the positions of methylation sites in E. coli chemoreceptors. White circles denote glycine residues in the glycine hinge between the stable (thick red) and unstable (thin red) helices of the flexible bundle. (C Upper) Model of higher-order receptor organization and the role of dimer bending in the kinase-on and -off states of receptor signaling complexes. (C Lower) A view from the tips of the trimers of dimers looking toward the cell membrane. The large gray circles denote the boundaries of the periplasmic-sensing domains in each signaling state. The green symbol represents an activated CheA molecule; the black symbol denotes a deactivated CheA.
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References

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