Functional correlation of bacterial LuxS with their quaternary associations: interface analysis of the structure networks.

ABSTRACT:

Background

The genome of a wide variety of prokaryotes contains the luxS gene homologue, which encodes for the protein S-ribosylhomocysteinelyase (LuxS). This protein is responsible for the production of the quorum sensing molecule, AI-2 and has been implicated in a variety of functions such as flagellar motility, metabolic regulation, toxin production and even in pathogenicity. A high structural similarity is present in the LuxS structures determined from a few species. In this study, we have modelled the structures from several other species and have investigated their dimer interfaces. We have attempted to correlate the interface features of LuxS with the phenotypic nature of the organisms.

Results

The protein structure networks (PSN) are constructed and graph theoretical

SUBMITTER: Bhattacharyya M 

PROVIDER: S-EPMC2656534 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature