Sandbox Reserved 1562
From Proteopedia
(Difference between revisions)
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<scene name='82/823086/Secondary_bap1/1'>Secondary Structure of Bap1 Creates Important Tertiary Structures</scene> | <scene name='82/823086/Secondary_bap1/1'>Secondary Structure of Bap1 Creates Important Tertiary Structures</scene> | ||
| - | Bap1 is a two-domain assembly which is made up of an eight-bladed β-propeller interrupted by a β-prism domain. The β-propeller domain is the larger of the two domains while the β-prism is the smaller of the two. The β-propeller is composed of 8 β-sheets with 3 greek keys present in between β-sheets 5 and 6 of the propeller. It is believed the lectin binding site is in the β-prism domain. | + | Bap1 is a two-domain assembly which is made up of an eight-bladed β-propeller interrupted by a β-prism domain. The β-propeller domain is the larger of the two domains while the β-prism is the smaller of the two. The β-propeller is composed of 8 β-sheets with 3 greek keys present in between β-sheets 5 and 6 of the propeller <ref name="Bap1">PMID:31439670</ref>. It is believed the lectin binding site is in the β-prism domain. |
| - | <scene name='82/823086/Important_aa/ | + | <scene name='82/823086/Important_aa/2'>Key Amino Acids in the Binding Pocket</scene> |
| - | There has not been a catalytic triad found for Bap1, but several amino acids are believed to play a role in the binding of citrate and carbohydrates. There are 6 amino acids believed to bind carbohydrates: Gly-344, Ala-345, Val-346 Asp-348, His-500, and Lys-501. With the exception of His-500, the other amino acids are structurally the same as the binding site of carbohydrates in RbmC. The binding site for citrate and carbohydrates is at the end of the β-prism which has a positively charged, <scene name='82/823086/Lys_in_active_site/1'>lysine-rich central cavity</scene>. | + | There has not been a catalytic triad found for Bap1, but several amino acids are believed to play a role in the binding of citrate and carbohydrates. There are 6 amino acids believed to bind carbohydrates: Gly-344, Ala-345, Val-346 Asp-348, His-500, and Lys-501 <ref name="Bap1"/>. With the exception of His-500, the other amino acids are structurally the same as the binding site of carbohydrates in RbmC. The amino acids interact with the substrate by either hydrogen bonding or Van der Waals forces. The binding site for citrate and carbohydrates is at the end of the β-prism which has a positively charged, <scene name='82/823086/Lys_in_active_site/1'>lysine-rich central cavity</scene>. |
<scene name='82/823086/Ligand_bap1/1'>Metal Binding Sites</scene> | <scene name='82/823086/Ligand_bap1/1'>Metal Binding Sites</scene> | ||
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There have been no energy transformations found for Bap1. | There have been no energy transformations found for Bap1. | ||
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| + | </StructureSection> | ||
== Citations == | == Citations == | ||
| - | + | <references/> | |
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Revision as of 05:07, 9 December 2019
| This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575. |
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Biofilm Associated Protein 1 (Bap1)
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Citations
- ↑ 1.0 1.1 Kaus K, Biester A, Chupp E, Lu J, Visudharomn C, Olson R. The 1.9 A crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion. J Biol Chem. 2019 Oct 4;294(40):14499-14511. doi: 10.1074/jbc.RA119.008335. Epub , 2019 Aug 22. PMID:31439670 doi:http://dx.doi.org/10.1074/jbc.RA119.008335
