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Proteins

Title:		"X-ray crystal structures of the pheromone-binding domains of two quorum-hindered transcription factors, YenR of Yersinia enterocolitica and CepR2 of Burkholderia cenocepacia"
Author(s):		Kim Y; Chhor G; Tsai CS; Fox G; Chen CS; Winans NJ; Jedrzejczak R; Joachimiak A; Winans SC;
Address:		"Midwest Center for Structural Genomics, Biosciences, Argonne National Laboratory, Argonne, Illinois, 60439. Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois, 60439. Department of Microbiology, Cornell University, Ithaca, New York, 14853. Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, 60637"
Journal Title:		Proteins
Year:		2017
Volume:		20170724
Issue:		10
Page Number:		1831 - 1844
DOI:		10.1002/prot.25336
ISSN/ISBN:		1097-0134 (Electronic) 0887-3585 (Print) 0887-3585 (Linking)
Abstract:		"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"
Keywords:		"Bacterial Proteins/*chemistry/genetics Burkholderia cenocepacia/chemistry Crystallography, X-Ray DNA-Binding Proteins/chemistry Gene Expression Regulation, Bacterial Homoserine/*analogs & derivatives/chemistry Lactones/*chemistry Pheromones/chemistry Prot;"
Notes:		"MedlineKim, Youngchang Chhor, Gekleng Tsai, Ching-Sung Fox, Gabriel Chen, Chia-Sui Winans, Nathan J Jedrzejczak, Robert Joachimiak, Andrzej Winans, Stephen C eng R24 GM115586/GM/NIGMS NIH HHS/ U54 GM094585/GM/NIGMS NIH HHS/ 2017/06/15 Proteins. 2017 Oct; 85(10):1831-1844. doi: 10.1002/prot.25336. Epub 2017 Jul 24"