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- Title
The structural basis of cyclic diguanylate signal transduction by PilZ domains.
- Authors
Benach, Jordi; Swaminathan, Swarup S; Tamayo, Rita; Handelman, Samuel K; Folta-Stogniew, Ewa; Ramos, John E; Forouhar, Farhad; Neely, Helen; Seetharaman, Jayaraman; Camilli, Andrew; Hunt, John F
- Abstract
The second messenger cyclic diguanylate (c-di-GMP) controls the transition between motile and sessile growth in eubacteria, but little is known about the proteins that sense its concentration. Bioinformatics analyses suggested that PilZ domains bind c-di-GMP and allosterically modulate effector pathways. We have determined a 1.9 A crystal structure of c-di-GMP bound to VCA0042/PlzD, a PilZ domain-containing protein from Vibrio cholerae. Either this protein or another specific PilZ domain-containing protein is required for V. cholerae to efficiently infect mice. VCA0042/PlzD comprises a C-terminal PilZ domain plus an N-terminal domain with a similar beta-barrel fold. C-di-GMP contacts seven of the nine strongly conserved residues in the PilZ domain, including three in a seven-residue long N-terminal loop that undergoes a conformational switch as it wraps around c-di-GMP. This switch brings the PilZ domain into close apposition with the N-terminal domain, forming a new allosteric interaction surface that spans these domains and the c-di-GMP at their interface. The very small size of the N-terminal conformational switch is likely to explain the facile evolutionary diversification of the PilZ domain.
- Publication
The EMBO journal, 2007, Vol 26, Issue 24, p5153
- ISSN
1460-2075
- Publication type
Journal Article
- DOI
10.1038/sj.emboj.7601918