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Title: Structure of GrlR and the Implication of its EDED Motif in Mediating the Regulation of Type III Secretion System in EHEC

Abstract

Enterohemorrhagic Escherichia coli (EHEC) is a common cause of severe hemorrhagic colitis. EHEC's virulence is dependent upon a type III secretion system (TTSS) encoded by 41 genes. These genes are organized in several operons clustered in the locus of enterocyte effacement. Most of the locus of enterocyte effacement genes, including grlA and grlR, are positively regulated by Ler, and Ler expression is positively and negatively modulated by GrlA and GrlR, respectively. However, the molecular basis for the GrlA and GrlR activity is still elusive. We have determined the crystal structure of GrlR at 1.9 Angstroms resolution. It consists of a typical {beta}-barrel fold with eight {beta}-strands containing an internal hydrophobic cavity and a plug-like loop on one side of the barrel. Strong hydrophobic interactions between the two {beta}-barrels maintain the dimeric architecture of GrlR. Furthermore, a unique surface-exposed EDED (Glu-Asp-Glu-Asp) motif is identified to be critical for GrlA-GrlR interaction and for the repressive activity of GrlR. This study contributes a novel molecular insight into the mechanism of GrlR function.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
960170
Report Number(s):
BNL-83156-2009-JA
TRN: US201016%%1314
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: PLoS Pathogens; Journal Volume: 3; Journal Issue: 5
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ARCHITECTURE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENES; REGULATIONS; RESOLUTION; SECRETION; VIRULENCE; national synchrotron light source

Citation Formats

Jobichen,C., Li, M., Yerushalmi, G., Tan, Y., Mok, Y., Rosenshine, I., Leung, K., and Sivaraman, J. Structure of GrlR and the Implication of its EDED Motif in Mediating the Regulation of Type III Secretion System in EHEC. United States: N. p., 2007. Web. doi:10.1371/journal.ppat.0030069.
Jobichen,C., Li, M., Yerushalmi, G., Tan, Y., Mok, Y., Rosenshine, I., Leung, K., & Sivaraman, J. Structure of GrlR and the Implication of its EDED Motif in Mediating the Regulation of Type III Secretion System in EHEC. United States. doi:10.1371/journal.ppat.0030069.
Jobichen,C., Li, M., Yerushalmi, G., Tan, Y., Mok, Y., Rosenshine, I., Leung, K., and Sivaraman, J. Mon . "Structure of GrlR and the Implication of its EDED Motif in Mediating the Regulation of Type III Secretion System in EHEC". United States. doi:10.1371/journal.ppat.0030069.
@article{osti_960170,
title = {Structure of GrlR and the Implication of its EDED Motif in Mediating the Regulation of Type III Secretion System in EHEC},
author = {Jobichen,C. and Li, M. and Yerushalmi, G. and Tan, Y. and Mok, Y. and Rosenshine, I. and Leung, K. and Sivaraman, J.},
abstractNote = {Enterohemorrhagic Escherichia coli (EHEC) is a common cause of severe hemorrhagic colitis. EHEC's virulence is dependent upon a type III secretion system (TTSS) encoded by 41 genes. These genes are organized in several operons clustered in the locus of enterocyte effacement. Most of the locus of enterocyte effacement genes, including grlA and grlR, are positively regulated by Ler, and Ler expression is positively and negatively modulated by GrlA and GrlR, respectively. However, the molecular basis for the GrlA and GrlR activity is still elusive. We have determined the crystal structure of GrlR at 1.9 Angstroms resolution. It consists of a typical {beta}-barrel fold with eight {beta}-strands containing an internal hydrophobic cavity and a plug-like loop on one side of the barrel. Strong hydrophobic interactions between the two {beta}-barrels maintain the dimeric architecture of GrlR. Furthermore, a unique surface-exposed EDED (Glu-Asp-Glu-Asp) motif is identified to be critical for GrlA-GrlR interaction and for the repressive activity of GrlR. This study contributes a novel molecular insight into the mechanism of GrlR function.},
doi = {10.1371/journal.ppat.0030069},
journal = {PLoS Pathogens},
number = 5,
volume = 3,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}