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: Biochemistry, Genetics and Molecular Biology > Molecular Biology
Divisions: Medicine > Vinayaka Mission's Kirupananda Variyar Medical College and Hospital, Salem > Biochemistry
Depositing User: Unnamed user with email techsupport@mosys.org
Last Modified: 10 Dec 2025 06:43
URI: https://vmuir.mosys.org/id/eprint/4112

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