Sandbox Reserved 1561: Difference between revisions
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<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 bonding. <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 bonding. <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. | <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. | ||
<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area. | <scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area. | ||
