Sandbox Reserved 1561: Difference between revisions

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<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/Key_bap1_residues/1'>Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located 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/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.

Sandbox Reserved 1561: Difference between revisions

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@@ Line 28: / Line 28: @@
 <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/Key_bap1_residues/1'>Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located 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/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.