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Title: The Structural Basis of Cyclic Diguanylate Signal Transduction by PilZ Domains

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 Angstroms 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.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959663
Report Number(s):
BNL-82649-2009-JA
Journal ID: ISSN 0261-4189; EMJODG; TRN: US201016%%807
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: EMBO Journal; Journal Volume: 26; Journal Issue: 24
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DIVERSIFICATION; MICE; PROTEINS; RESIDUES; national synchrotron light source

Citation Formats

Benach,J., Swaminathan, S., Tamayo, R., Handelman, S., Folta-Stogniew, E., Ramos, J., Forouhar, F., Neely, H., Seetharaman, J., and et al. The Structural Basis of Cyclic Diguanylate Signal Transduction by PilZ Domains. United States: N. p., 2007. Web. doi:10.1038/sj.emboj.7601918.
Benach,J., Swaminathan, S., Tamayo, R., Handelman, S., Folta-Stogniew, E., Ramos, J., Forouhar, F., Neely, H., Seetharaman, J., & et al. The Structural Basis of Cyclic Diguanylate Signal Transduction by PilZ Domains. United States. doi:10.1038/sj.emboj.7601918.
Benach,J., Swaminathan, S., Tamayo, R., Handelman, S., Folta-Stogniew, E., Ramos, J., Forouhar, F., Neely, H., Seetharaman, J., and et al. Mon . "The Structural Basis of Cyclic Diguanylate Signal Transduction by PilZ Domains". United States. doi:10.1038/sj.emboj.7601918.
@article{osti_959663,
title = {The Structural Basis of Cyclic Diguanylate Signal Transduction by PilZ Domains},
author = {Benach,J. and Swaminathan, S. and Tamayo, R. and Handelman, S. and Folta-Stogniew, E. and Ramos, J. and Forouhar, F. and Neely, H. and Seetharaman, J. and et al},
abstractNote = {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 Angstroms 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.},
doi = {10.1038/sj.emboj.7601918},
journal = {EMBO Journal},
number = 24,
volume = 26,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}