Publication: Structural insights into RbmA, a biofilm scaffolding protein of V. cholerae
| cris.lastimport.scopus | 2025-05-09T22:33:05Z | |
| cris.virtual.department | Chemistry | en_US |
| cris.virtual.orcid | 0000-0002-9566-7216 | en_US |
| cris.virtualsource.department | 31cb22d6-8626-4d4f-8689-62e2d6e45d1b | |
| cris.virtualsource.orcid | 31cb22d6-8626-4d4f-8689-62e2d6e45d1b | |
| dc.contributor.author | MANUEL MAESTRE-REYNA | en_US |
| dc.contributor.author | Wu W.-J | en_US |
| dc.contributor.author | Wang A.H.-J. | en_US |
| dc.creator | Maestre-Reyna M;Wu W.-J;Wang A.H.-J. | |
| dc.date.accessioned | 2022-11-11T03:00:22Z | |
| dc.date.available | 2022-11-11T03:00:22Z | |
| dc.date.issued | 2013 | |
| dc.description.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. | |
| dc.identifier.doi | 10.1371/journal.pone.0082458 | |
| dc.identifier.issn | 19326203 | |
| dc.identifier.pmid | 24340031 | |
| dc.identifier.scopus | 2-s2.0-84891933587 | |
| dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84891933587&doi=10.1371%2fjournal.pone.0082458&partnerID=40&md5=82ab054295a82a42f9137be469b99cda | |
| dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/624883 | |
| dc.relation.ispartof | PLoS ONE | |
| dc.relation.journalissue | 12 | |
| dc.relation.journalvolume | 8 | |
| dc.subject.other | 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 | |
| dc.title | Structural insights into RbmA, a biofilm scaffolding protein of V. cholerae | en_US |
| dc.type | journal article | en |
| dspace.entity.type | Publication |