Sandbox Reserved 1561: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 34: | Line 34: | ||
<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. | ||
<scene name='82/823085/Asp348/1'>Asp348</scene>is the key residue of carbohydrate bonding. The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller. | <scene name='82/823085/Asp348/1'>Asp348</scene> is the key amino acid residue of 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> The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller. | ||
== Energy Transformation == | == Energy Transformation == | ||
