Sandbox Reserved 1562

Function and Bioligical Relevance

Bap1 is one of the major extracellular matrix proteins found in the bacterium Vibrio Cholerae and functions in biofilm architecture and surface attachment. Bap1 is composed of two domains, a β-propeller domain, and a β-prism domain.

Implications

The function of Bap1 should be researched more to help us understand how cholera infects/spreads in contaminated water and food. Infected food/water with "V. Cholerae" can cause cholera if contaminated water or food is consumed. Treatment for cholera is getting more challenging with the increasing use of the antibiotics and the bacterium becoming more resistant to the treatment. This is a big issue considering there are millions of people that don't have access to clean drinking water. With more research on how Bap1 functions in V. Cholerae, the spreading of cholera will be understood better and should be able to be controlled better.

Structural highlights

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. It is believed the lectin binding site is in between the β-sheets of the β-propeller.

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