상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Crystal structure of SmcR, a quorum-sensing master regulator of Vibrio vulnificus, provides insight into its regulation of transcription

Authors 

Y KimB S KimY J ParkWon Chan ChoiJung-Won HwangB S KangTae Kwang OhS H ChoiMyung Hee Kim

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2010

Citation 

Journal of Biological Chemistry, vol. 285, no. 18, pp. 14020-14030

Keywords 

Bacterial pathogensBinding residuesDimerization domainDNA recognitionHuman pathogensIn-vitroIn-vivoMaster regulatorsN-terminalsProtein structuresProtein-DNA interactionsQuorum-sensingRegulation of transcriptionRegulatory functionsRegulatory systemsSophisticated mechanismVibrio vulnificusVirulence factors

Abstract 

Quorum sensing has been implicated as an important global regulatory system controlling the expression of numerous virulence factors in bacterial pathogens. SmcR, a homologue of Vibrio harveyi LuxR, has been proposed as a quorum-sensing master regulator of Vibrio vulnificus, an opportunistic human pathogen. Previous studies demonstrated that SmcR is essential for the survival and pathogenesis of V. vulnificus, indicating that inhibiting SmcR is an attractive approach to combat infections by the bacteria. Here, we determined the crystal structure of SmcR at 2.1 ? resolution. The protein structure reveals a typical TetR superfamily fold consisting of an N-terminalDNAbinding domain and a C-terminal dimerization domain. In vivo and in vitro functional analysis of the dimerization domain suggested that dimerization of SmcR is vital for its biological regulatory function. The N-terminal DNA recognition and binding residues were assigned based on the protein structure and the results of in vivo and in vitro mutagenesis experiments. Furthermore, protein-DNA interaction experiments suggested that SmcRmay have a sophisticated mechanism that enables the protein to recognize each of its many target operators with different affinities.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M109.100248

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)