Sandbox Reserved 1561: Difference between revisions

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<scene name='82/823085/Isolated_beta-prism_view/1'> Beta-Prism View</scene> "The Bap1 Beta-prism falls into the jacalin-related (JRL) protein family, which consists of a pseudo-3-fold arrangement of Greek key motifs." <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> The beta-prism is located on blade six of the beta-propeller of Bap1 from V. cholerae. Bap1 beta-prism binds carbohydrate ligands along with citrate ions at a single sugar site. This binding process contributes to the crystal structure of Bap1.
<scene name='82/823085/Isolated_beta-prism_view/1'> Beta-Prism View</scene> "The Bap1 Beta-prism falls into the jacalin-related (JRL) protein family, which consists of a pseudo-3-fold arrangement of Greek key motifs." <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> The beta-prism is located on blade six of the beta-propeller of Bap1 from V. cholerae. Bap1 beta-prism binds carbohydrate ligands along with citrate ions at a single sugar site. This binding process contributes to the crystal structure of Bap1.


<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.  
<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>


<scene name='82/823085/Active_binding_sites/1'> Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.
<scene name='82/823085/Active_binding_sites/1'> Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.
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