6MLT
Crystal structure of the V. cholerae biofilm matrix protein Bap1
Summary for 6MLT
| Entry DOI | 10.2210/pdb6mlt/pdb |
| Descriptor | Hemolysin-related protein, CALCIUM ION, SODIUM ION, ... (6 entities in total) |
| Functional Keywords | biofilm matrix protein, carbohydrate-binding protein, metal-binding protein, secreted protein, sugar binding protein |
| Biological source | Vibrio cholerae serotype O1 |
| Total number of polymer chains | 1 |
| Total formula weight | 66806.21 |
| Authors | Kaus, K.,Biester, A.,Chupp, E.,Lu, K.,Vidsudharomn, C.,Olson, R. (deposition date: 2018-09-28, release date: 2019-08-28, Last modification date: 2024-03-13) |
| Primary citation | Kaus, K.,Biester, A.,Chupp, E.,Lu, J.,Visudharomn, C.,Olson, R. The 1.9 angstrom crystal structure of the extracellular matrix protein Bap1 fromVibrio choleraeprovides insights into bacterial biofilm adhesion. J.Biol.Chem., 294:14499-14511, 2019 Cited by PubMed Abstract: Growth of the cholera bacterium in a biofilm community contributes to both its pathogenicity and survival in aquatic environmental niches. The major components of biofilms include olyaccharide (VPS) and the extracellular matrix proteins RbmA, RbmC, and Bap1. To further elucidate the previously observed overlapping roles of Bap1 and RbmC in biofilm architecture and surface attachment, here we investigated the structural and functional properties of Bap1. Soluble expression of Bap1 was possible only after the removal of an internal 57-amino-acid-long hydrophobic insertion sequence. The crystal structure of Bap1 at 1.9 Å resolution revealed a two-domain assembly made up of an eight-bladed β-propeller interrupted by a β-prism domain. The structure also revealed metal-binding sites within canonical calcium blade motifs, which appear to have structural rather than functional roles. Contrary to results previously observed with RbmC, the Bap1 β-prism domain did not exhibit affinity for complex -glycans, suggesting an altered role of this domain in biofilm-surface adhesion. Native polyacrylamide gel shift analysis did suggest that Bap1 exhibits lectin activity with a preference for anionic or linear polysaccharides. Our results suggest a model for biofilms in which Bap1 and RbmC play dominant but differing adhesive roles in biofilms, allowing bacterial attachment to diverse environmental or host surfaces. PubMed: 31439670DOI: 10.1074/jbc.RA119.008335 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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