|Title:||Structural insights into RbmA, a biofilm scaffolding protein of V. cholerae||Authors:||MANUEL MAESTRE-REYNA
|Issue Date:||2013||Journal Volume:||8||Journal Issue:||12||Source:||PLoS ONE||Abstract:||
V. cholerae can form sessile biofilms associated with abiotic surfaces, cyanobacteria, zoo-plankton, mollusks, or crustaceans. Along with the vibrio polysaccharide, secreted proteins of the rbm gene cluster are key to the biofilm ultrastructure. Here we provide a thorough structural characterization of RbmA, a protein involved in mediating cellcell and cell-biofilm contacts. We correlate our structural findings with initial ligand specificity screening results, NMR protein-ligand interaction analysis, and complement our results with a full biocomputational study. © 2013 Maestre-Reyna et al.
|ISSN:||19326203||DOI:||10.1371/journal.pone.0082458||SDG/Keyword:||protein RbmA; scaffold protein; unclassified drug; amino acid sequence; article; biofilm; cell contact; crystallization; Escherichia coli; molecular cloning; molecular docking; molecular dynamics; nonhuman; nuclear magnetic resonance; protein interaction; protein purification; protein structure; sequence alignment; Vibrio cholerae; Bacterial Proteins; Biofilms; Ligands; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; Structure-Activity Relationship; Vibrio cholerae|
|Appears in Collections:||化學系|
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