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X-ray crystal structures of the pheromone-binding domains of two quorum-hindered transcription factors, YenR of Yersinia enterocolitica and CepR2 of Burkholderia cenocepacia: KIM et al.

Journal Article · · Proteins
DOI:https://doi.org/10.1002/prot.25336· OSTI ID:1393501
 [1];  [2];  [3];  [3];  [3];  [3];  [4];  [5];  [3]
  1. Midwest Center for Structural Genomics, Biosciences, Argonne National Laboratory, Argonne Illinois 60439; Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne Illinois 60439
  2. Midwest Center for Structural Genomics, Biosciences, Argonne National Laboratory, Argonne Illinois 60439
  3. Department of Microbiology, Cornell University, Ithaca New York 14853
  4. Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne Illinois 60439
  5. Midwest Center for Structural Genomics, Biosciences, Argonne National Laboratory, Argonne Illinois 60439; Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne Illinois 60439; Department of Biochemistry and Molecular Biology, University of Chicago, Chicago Illinois 60637
The ability of LuxR-type proteins to regulate transcription is controlled by bacterial pheromones, N-acylhomoserine lactones (AHLs). Most LuxR-family proteins require their cognate AHLs for activity, and some of them require AHLs for folding and stability, and for protease-resistance. However, a few members of this family are able to fold, dimerize, bind DNA, and regulate transcription in the absence of AHLs; moreover, these proteins are antagonized by their cognate AHLs. One such protein is YenR of Yersinia enterocolitica, which is antagonized by N-3-oxohexanoyl-l-homoserine lactone (OHHL). This pheromone is produced by the OHHL synthase, a product of the adjacent yenI gene. Another example is CepR2 of Burkholderia cenocepacia, which is antagonized by N-octanoyl-l-homoserine lactone (OHL), whose synthesis is directed by the cepI gene of the same bacterium. Here, we describe the high-resolution crystal structures of the AHL binding domains of YenR and CepR2. YenR was crystallized in the presence and absence of OHHL. While this ligand does not cause large scale changes in the YenR structure, it does alter the orientation of several highly conserved YenR residues within and near the pheromone-binding pocket, which in turn caused a significant movement of a surface-exposed loop.
Research Organization:
Argonne National Laboratory (ANL)
Sponsoring Organization:
National Institutes of Health (NIH); USDOE Office of Science - Office of Biological and Environmental Research
DOE Contract Number:
AC02-06CH11357
OSTI ID:
1393501
Journal Information:
Proteins, Journal Name: Proteins Journal Issue: 10 Vol. 85; ISSN 0887-3585
Publisher:
Wiley
Country of Publication:
United States
Language:
English

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