Structure of GrlR-GrlA complexStructure of GrlR-GrlA complex

Structural highlights

4kt5 is a 3 chain structure with sequence from Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7DB61_ECO57

Publication Abstract from PubMed

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-GrlADelta (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.

Structure of GrlR-GrlA complex that prevents GrlA activation of virulence genes.,Padavannil A, Jobichen C, Mills E, Velazquez-Campoy A, Li M, Leung KY, Mok YK, Rosenshine I, Sivaraman J Nat Commun. 2013 Oct 4;4:2546. doi: 10.1038/ncomms3546. PMID:24092262[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Padavannil A, Jobichen C, Mills E, Velazquez-Campoy A, Li M, Leung KY, Mok YK, Rosenshine I, Sivaraman J. Structure of GrlR-GrlA complex that prevents GrlA activation of virulence genes. Nat Commun. 2013 Oct 4;4:2546. doi: 10.1038/ncomms3546. PMID:24092262 doi:http://dx.doi.org/10.1038/ncomms3546

4kt5, resolution 2.70Å

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