Sandbox Reserved 1562

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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 -->
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==Your Heading Here (maybe something like 'Structure')==
 
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
 
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
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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.
 
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== Function(s) and Biological Relevance ==
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==Biofilm Associated Protein 1 (Bap1)==
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== Broader Implications ==
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<StructureSection load='6mlt' size='340' side='right' caption='Bap1' scene=''>
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== Structural highlights and structure-function relationships ==
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== Function and Bioligical Relevance ==
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Bap1 is one of the major extracellular matrix proteins along with RbmA and RbmC. These proteins are 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.
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== Implications ==
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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 an estimated 2.9 million cases and almost 100,000 deaths per year <ref>https://www.cdc.gov/cholera/general/index.html</ref>. 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.
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== Structural highlights ==
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<scene name='82/823086/Secondary_bap1/1'>Secondary Structure of Bap1 Creates Important Tertiary Structures</scene>
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Bap1 is a two-domain assembly which is made up of an <scene name='82/823086/Beta_propeller/2'>eight-bladed β-propeller</scene> 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 <ref name="Bap1">PMID:31439670</ref>. It is believed the lectin binding site is in the β-prism domain.
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<scene name='82/823086/Important_aa/2'>Key Amino Acids in the Binding Pocket</scene>
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There has not been a catalytic triad found for Bap1, but several amino acids are believed to play a role in the binding of citrate and carbohydrates. There are 6 amino acids believed to bind carbohydrates: Gly-344, Ala-345, Val-346 Asp-348, His-500, and Lys-501 <ref name=" Bap1"/>. With the exception of His-500, the other amino acids are structurally the same as the binding site of carbohydrates in RbmC. The amino acids interact with the substrate by either hydrogen bonding or Van der Waals forces. The binding site for citrate and carbohydrates is at the end of the β-prism which has a positively charged, <scene name='82/823086/Lys_in_active_site/1'>lysine-rich central cavity</scene>.
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<scene name='82/823086/Metal_binding/1'>Metal Binding Sites</scene>
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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 <ref name= "Bap1"/>
== Energy Transformation ==
== Energy Transformation ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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Since the function of Bap1 is to attach biofilms together, there is no energy transformation for this protein.
</StructureSection>
</StructureSection>
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== References ==
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== Citations ==
<references/>
<references/>

Current revision

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:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Biofilm Associated Protein 1 (Bap1)

Bap1

Drag the structure with the mouse to rotate

Citations

  1. ↑ https://www.cdc.gov/cholera/general/index.html
  2. ↑ 2.0 2.1 2.2 Kaus K, Biester A, Chupp E, Lu J, Visudharomn C, Olson R. The 1.9 A crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion. J Biol Chem. 2019 Oct 4;294(40):14499-14511. doi: 10.1074/jbc.RA119.008335. Epub , 2019 Aug 22. PMID:31439670 doi:http://dx.doi.org/10.1074/jbc.RA119.008335
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