Sandbox CHEM351F19TH
From Proteopedia
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| + | <Structure load='6mlt' size='350' frame='true' align='right' caption='Bap1' scene='Cartoon Model' /> | ||
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==6MLT== | ==6MLT== | ||
| - | <scene name='82/827835/6mlt_transparent/1'>6MLT Transparent</scene><StructureSection load='6mlt' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | <scene name='82/827835/Bap1/1'>Bap1</scene> | ||
== Function == | == Function == | ||
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| - | Bap1 is one of the major extracellular matrix proteins found in ''Vibrio cholerae'' and functions in biofilm architecture and surface attachment. | + | Bap1 is one of the major extracellular matrix proteins found in the bacterium ''Vibrio cholerae'' and functions in biofilm architecture and surface attachment. SUBSTRATE AND PRODUCT. |
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== Structural highlights == | == Structural highlights == | ||
| - | + | There is a two-domain assembly which is made up of an eight-bladed β-propeller interrupted by a β-prism domain. There are metal-binding sites, which appear to help more with the structure of the protein than the function of it. Bap1 exhibits lectin activity and is believed anionic or linear polysaccharides are preferred. | |
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== Energy Transformation == | == Energy Transformation == | ||
Current revision
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Contents |
6MLT
Function
Bap1 is one of the major extracellular matrix proteins found in the bacterium Vibrio cholerae and functions in biofilm architecture and surface attachment. SUBSTRATE AND PRODUCT.
Implications
Structural highlights
There is a two-domain assembly which is made up of an eight-bladed β-propeller interrupted by a β-prism domain. There are metal-binding sites, which appear to help more with the structure of the protein than the function of it. Bap1 exhibits lectin activity and is believed anionic or linear polysaccharides are preferred.
