Sandbox Reserved 1561: Difference between revisions
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<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/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/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate | <scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate binding. <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/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<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> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site. The active site of Bap1 is outside of its central cavity of the eight-bladed beta-propeller and doesn't yield a catalytic triad.<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/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<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> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site. The active site of Bap1 is outside of its central cavity of the eight-bladed beta-propeller and doesn't yield a catalytic triad.<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> | ||
