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Sandbox Reserved 1459

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Revision as of 06:20, 15 November 2018

This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470.

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Click the edit this page tab at the top. Save the page after each step, then edit it again.
Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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.

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VesB

1 Function
2 Disease
3 Relevance
4 Structural highlights

Function

^[1] is a serine protease that is found in the bacteria Vibrio cholerae. The function of VesB is to contribute to intestinal growth and pathogenesis. VesB is also able to cleave peptide bonds in proteins after arginines. This means that the substrate of VesB would be a protein containing arginine, or multiple arginines (XXRXX) and the product after cleavage is all of the protein through the arginine, and the rest of the protein(XXR + XX), or the rest of the protein through the next arginine, if there are multiple.

Disease

VesB has been detected in vibrio cholerae from patients with clinical cholera. VesB is able to cleave the A subunit of cholera toxin, which is a process that leads to the activation of cholera toxin. Cholera toxin is then released into the intestine, causing Cholera. When the toxin is released, it causes rapid fluid loss and severe dehydration.

Relevance

Structural highlights

VesB's is made up mostly of beta sheets with some alpha helices and random coil. VesB has that make up it's tertiary/quaternary structure. It has a N-terminal protease domain with a trypsin/chymotrypsin-fold and a C-terminal Ig-fold domain. Although VesB's structure does not seem very large, looking at a of VesB shows a more accurate view of how large VesB is and how much space it actually takes up. VesB has few regions on it's structure, including the active site. These hydrophobic regions are important because they show where the active site is located, and the hydrophilic regions show where the alpha helices are located, since they are hydrophilic on the outside, and have a hydrophobic core.The hydrophilic regions also show where water would most likely be attracted to, and because there are so many hydrophilic regions, it would show that a great amount of water would be attracted to VesB.

This crystal structure was solved without a ligand, but the VesB ligand is known to be any protein containing Arg-X.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

↑ Gadwal S, Korotkov KV, Delarosa JR, Hol WG, Sandkvist M. Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB. J Biol Chem. 2014 Jan 23. PMID:24459146 doi:http://dx.doi.org/10.1074/jbc.M113.525261

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1459"

@@ Line 14: / Line 14: @@
 == Structural highlights ==
-VesB's <scene name='79/799587/Secondary_structure/1'>secondary structure</scene> is made up mostly of beta sheets with some alpha helices and random coil. VesB has <scene name='79/799587/Two_domains/2'>two domains</scene> that make up it's tertiary/quaternary structure. It has a N-terminal protease domain with a trypsin/chymotrypsin-fold and a C-terminal Ig-fold domain. Although VesB's structure does not seem very large, looking at a <scene name='79/799587/Space-filling_view/1'>space-filling view</scene> of VesB shows a more accurate view of how large VesB is and how much space it actually takes up.
+VesB's <scene name='79/799587/Secondary_structure/1'>secondary structure</scene> is made up mostly of beta sheets with some alpha helices and random coil. VesB has <scene name='79/799587/Two_domains/2'>two domains</scene> that make up it's tertiary/quaternary structure. It has a N-terminal protease domain with a trypsin/chymotrypsin-fold and a C-terminal Ig-fold domain. Although VesB's structure does not seem very large, looking at a <scene name='79/799587/Space-filling_view/1'>space-filling view</scene> of VesB shows a more accurate view of how large VesB is and how much space it actually takes up. VesB has few <scene name='79/799587/Hydrophobicity/2'>hydrophobic</scene> regions on it's structure, including the active site. These hydrophobic regions are important because they show where the active site is located, and the hydrophilic regions show where the alpha helices are located, since they are hydrophilic on the outside, and have a hydrophobic core.The hydrophilic regions also show where water would most likely be attracted to, and because there are so many hydrophilic regions, it would show that a great amount of water would be attracted to VesB.
-<scene name='79/799587/Hydrophobicity/1'>Hydrophobicity</scene>
 This crystal structure was solved without a ligand, but the VesB ligand is known to be any protein containing Arg-X.

Sandbox Reserved 1459

From Proteopedia

Revision as of 06:20, 15 November 2018

VesB

Contents

Function

Disease

Relevance

Structural highlights

References

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