https://scholars.lib.ntu.edu.tw/handle/123456789/624883| Title: | Structural insights into RbmA, a biofilm scaffolding protein of V. cholerae | Authors: | MANUEL MAESTRE-REYNA Wu W.-J Wang A.H.-J. |
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. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84891933587&doi=10.1371%2fjournal.pone.0082458&partnerID=40&md5=82ab054295a82a42f9137be469b99cda https://scholars.lib.ntu.edu.tw/handle/123456789/624883 |
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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