TY - JOUR
T1 - Structural insights into RbmA, a biofilm scaffolding protein of V. cholerae
AU - Maestre-Reyna, Manuel
AU - Wu, Wen Jin
AU - Wang, Andrew H.J.
N1 - Funding Information:
The authors would like to thank Academia Sinica for support, the National Synchrotron Radiation Research Center of Taiwan, and Spring-8 for beam time allocations, the Core Facility for Protein Structural Analysis (grant #NSC 101-2319-B-001-003) for use of its crystallization facility, Prof. Lars-Oliver Essen (Philipps University Marburg) and the National Center for High-Performance Computing for computing time allocation, and Dr. David Smith and the Consortium for Functional glycomics for performing in vitro screening of glycan specificity (CFG request # 2666). The NMR spectra were obtained at the Core Facility for Protein Structural Analysis supported by National Core facility Program for Biotechnology.
PY - 2013/12/5
Y1 - 2013/12/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84891933587&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84891933587&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0082458
DO - 10.1371/journal.pone.0082458
M3 - Article
C2 - 24340031
AN - SCOPUS:84891933587
SN - 1932-6203
VL - 8
JO - PLoS ONE
JF - PLoS ONE
IS - 12
M1 - e82458
ER -