Sandbox Reserved 1562
From Proteopedia
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{{Sandbox_Reserved_BHall_Chem351_F19}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_Chem351_F19}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | ==Your Heading Here (maybe something like 'Structure')== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Function(s) and Biological Relevance == | ||
| - | == | + | <Structure load='6mlt' size='350' frame='true' align='right' caption='Bap1' scene='Cartoon Model' /> |
| - | == | + | ==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. | |
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| + | == Implications == | ||
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| + | == Structural highlights == | ||
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| + | 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 == | ||
| - | + | == Citations == | |
| - | == | + | |
<references/> | <references/> | ||
Revision as of 02:47, 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 |
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.
