Sandbox Reserved 1562
From Proteopedia
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The metal-binding sites in Bap1 are believed to only have a structural purpose and little to no effect on the function of the protein. | The metal-binding sites in Bap1 are believed to only have a structural purpose and little to no effect on the function of the protein. | ||
| + | Catalytic Triad | ||
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| + | There has not been a catalytic triad found for Bap1. | ||
== Energy Transformation == | == Energy Transformation == | ||
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== Citations == | == Citations == | ||
| - | Kaus, K., Biester, A., Chupp, E., Lu, J., Visudharomn, C., & Olson, R. (2019). The 1.9 Å crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion. Journal of Biological Chemistry, 294(40), 14499–14511. | + | Kaus, K., Biester, A., Chupp, E., Lu, J., Visudharomn, C., & Olson, R. (2019). The 1.9 Å crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion. Journal of Biological Chemistry, 294(40), 14499–14511. DOI: 10.1074/jbc.ra119.008335 |
Revision as of 07:13, 1 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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Contents |
Bap1
Function
Bap1 is one of the major extracellular matrix proteins found in the bacterium Vibrio Cholerae and functions in biofilm architecture and surface attachment. The protein binds mainly to carbohydrates and citrate anions but also has many binding pockets for different metals. V. Cholerae can cause cholera if contaminated water or food is consumed.
Implications
The function of Bap1 should be researched more to help us understand how cholera infects/spreads in water and food. Water infected with "V. Cholerae" can be fatal if left untreated. Treatment for cholera is getting more challenging with the increasing use of the antibiotics and the bacterium becoming more resistant to the treatment.
Structural highlights
There 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. There are metal-binding sites, which appear to help more with the structure of the protein than the function of it.
It is believed the lectin binding site is in between the β-sheets of the β-propeller. In between β-sheets 5 and 6 of the β-propeller, there are 3 greek keys also present.
The metal-binding sites in Bap1 are believed to only have a structural purpose and little to no effect on the function of the protein.
Catalytic Triad
There has not been a catalytic triad found for Bap1.
Energy Transformation
There have been no energy transformations found for Bap1.
Citations
Kaus, K., Biester, A., Chupp, E., Lu, J., Visudharomn, C., & Olson, R. (2019). The 1.9 Å crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion. Journal of Biological Chemistry, 294(40), 14499–14511. DOI: 10.1074/jbc.ra119.008335
