Sandbox CHEM351F19TH

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (02:42, 1 December 2019) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
 +
<Structure load='6mlt' size='350' frame='true' align='right' caption='Bap1' scene='Cartoon Model' />
 +
==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>
 
-
This is a default text for your page '''Sandbox CHEM351F19TH'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; 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 ==
== 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 ==
== Implications ==
Line 11: Line 12:
== Structural highlights ==
== Structural highlights ==
-
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.
+
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.
-
 
+
-
</StructureSection>
+
== Energy Transformation ==
== Energy Transformation ==

Current revision

Bap1

Drag the structure with the mouse to rotate

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.

Energy Transformation

Citations

Personal tools