Molecular modeling and active site analysis of SdiA homolog, a putative quorum sensor for Salmonella typhimurium pathogenecity reveals specific binding patterns of AHL transcriptional regulators

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Gnanendra, Shanmugam and Anusuya, Shanmugam and Natarajan, Jeyakumar (2012) Molecular modeling and active site analysis of SdiA homolog, a putative quorum sensor for Salmonella typhimurium pathogenecity reveals specific binding patterns of AHL transcriptional regulators. Journal of Molecular Modeling, 18 (10). pp. 4709-4719. ISSN 1610-2940

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Abstract

This study analyzed Salmonella typhimurium SdiA homolog, a LuxR family quorum sensor. Structural homology showed conserved residues W67, D80, and Y71 for hydrogen bonding and hydrophobic interactions with acyl homoserine lactones (AHL). Additionally, R60 enhances binding with AHL autoinducers. These findings guide enzymatic studies and design of inhibitors against S. typhimurium pathogenicity. © Springer-Verlag 2012. © 2013 Elsevier B.V., All rights reserved.

Item Type: Article
Subjects: Chemistry > Catalysis
Chemistry > Inorganic Chemistry
Chemistry > Organic Chemistry
Chemistry > Physical and Theoretical Chemistry
Computer Science > Computer Science Applications
Computer Science > Computational Theory and Mathematics
Divisions: Dentistry > Vinayaka Mission‘s Sankarachariyar Dental College, Salem > Oral Pathology
Depositing User: Unnamed user with email techsupport@mosys.org
Last Modified: 10 Dec 2025 06:43
URI: https://ir.vmrfdu.edu.in/id/eprint/4112

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