4KT5

Structure of GrlR-GrlA complex

Summary for 4KT5

• Entry DOI: 10.2210/pdb4kt5/pdb
• Descriptor: GrlR, GrlA, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: beta barrel, hth motif, regulator, transcription regulator
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 45500.54

Authors

Padavannil, A.,Jobichen, C.,Sivaraman, J. (deposition date: 2013-05-20, release date: 2013-10-09, Last modification date: 2024-10-30)

Primary citation

Padavannil, A.,Jobichen, C.,Mills, E.,Velazquez-Campoy, A.,Li, M.,Leung, K.Y.,Mok, Y.K.,Rosenshine, I.,Sivaraman, J.
Structure of GrlR-GrlA complex that prevents GrlA activation of virulence genes
Nat Commun, 4:2546-2546, 2013

PubMed Abstract: The locus of enterocyte effacement (LEE) is essential for virulence of enterohaemorrhagic Escherichia coli (EHEC) and enteropathogenic E. coli (EPEC). The 41 genes of the LEE encode type III secretion system proteins and three associated regulators: Ler, GrlA and GrlR. Ler is a positive regulator for most of the LEE operons, including grlRA. GrlA controls the expression of ler, ehxCABD and flhDC operons. GrlR binds to GrlA and suppresses its function. Here we report the crystal structure of GrlR-GrlAΔ (aa 1-106) complex (2:1) and its functional characterization. We show that GrlR interacts with the Helix-Turn-Helix motif of GrlA. Moreover, GrlA binds to the promoter DNA fragments of ler, ehxCABD and flhDC, and GrlR outcompetes with these promoter DNA sequences for the Helix-Turn-Helix motif of GrlA. These findings provide mechanistic insight into a regulatory module for the virulence of EPEC and EHEC, two important pathogens that cause devastating diseases.

PubMed: 24092262
DOI: 10.1038/ncomms3546

Experimental method

X-RAY DIFFRACTION (2.7 Å)