Sandbox Reserved 1561: Difference between revisions

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<scene name='82/823085/Eight-bladed_beta-propeller/2'>Eight-Bladed Beta-Propeller</scene> The eight-bladed beta-propeller has a four-stranded antiparallel beta-sheet making up each blade along with a beta-prism attached int he loop of blade six of the beta propeller. The Bap1 beta-propeller is a metal binding site, structural stability promotor, adhesion promoter, and aids in solubility and expression of the protein. <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/Beta-prism_binding_site/1'>Beta-Prism</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 ~~thy~~ crystal structure of Bap1.

<scene name='82/823085/Beta-prism_binding_site/1'>Beta-Prism</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.

Sandbox Reserved 1561: Difference between revisions

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 <scene name='82/823085/Eight-bladed_beta-propeller/2'>Eight-Bladed Beta-Propeller</scene> The eight-bladed beta-propeller has a four-stranded antiparallel beta-sheet making up each blade along with a beta-prism attached int he loop of blade six of the beta propeller. The Bap1 beta-propeller is a metal binding site, structural stability promotor, adhesion promoter, and aids in solubility and expression of the protein. <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/Beta-prism_binding_site/1'>Beta-Prism</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 thy crystal structure of Bap1.
+<scene name='82/823085/Beta-prism_binding_site/1'>Beta-Prism</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.