4be5

V. cholera biofilm scaffolding protein RbmA

spinqualitylabelsall models 4be5, resolution 2.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4be5 is a 2 chain structure with sequence from Vibrio cholerae MJ-1236. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.46Å Ligands: GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 cell-cell 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. Structural Insights into RbmA, a Biofilm Scaffolding Protein of V. Cholerae.,Maestre-Reyna M, Wu WJ, Wang AH PLoS One. 2013 Dec 5;8(12):e82458. doi: 10.1371/journal.pone.0082458. PMID:24340031 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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