Sandbox Reserved 1562
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
==Biofilm Associated Protein 1 (Bap1)== | ==Biofilm Associated Protein 1 (Bap1)== | ||
| - | <StructureSection load='6mlt' size='340' side='right' caption=' | + | <StructureSection load='6mlt' size='340' side='right' caption='Bap1' scene=''> |
| - | + | ||
== Function and Bioligical Relevance == | == 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. | + | Bap1 is one of the major extracellular matrix proteins found in the bacterium ''Vibrio Cholerae'' and functions in biofilm architecture and surface attachment. ''V. Cholerae'' is involved in the progression of cholera. Bap1 is composed of two domains, a β-propeller domain, and a β-prism domain. The main role of the protein is to bind citrate and carbohydrates, which occurs in the binding pocket of the β-prism domain. |
== Implications == | == Implications == | ||
| Line 18: | Line 17: | ||
<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. It is believed the lectin binding site is in between the β-sheets of the β-propeller. | + | 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 between the β-sheets of the β-propeller. |
<scene name='82/823086/Ligand_bap1/1'>Metal Binding Sites</scene> | <scene name='82/823086/Ligand_bap1/1'>Metal Binding Sites</scene> | ||
Revision as of 01:34, 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. |
To get started:
More help: Help:Editing |
Biofilm Associated Protein 1 (Bap1)
| |||||||||||
