Sandbox Reserved 1461
From Proteopedia
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The role of this protein is to help with the prevention and survival of diseases. VesB has been detected in in V. Cholerae which has been isolated from stools of patients with clinical cholera. It is believed that it helps in intestinal growth of V. cholerae because it is found in V. cholerae. VesB is able to split the A subunit of choleratoxin. There is a chance that it helps in intestinal growth of V. cholerae. VesB is able to split the A subunit of choleratoxin. | The role of this protein is to help with the prevention and survival of diseases. VesB has been detected in in V. Cholerae which has been isolated from stools of patients with clinical cholera. It is believed that it helps in intestinal growth of V. cholerae because it is found in V. cholerae. VesB is able to split the A subunit of choleratoxin. There is a chance that it helps in intestinal growth of V. cholerae. VesB is able to split the A subunit of choleratoxin. | ||
== Relevance == | == Relevance == | ||
| + | Since VesB has the potential to help with intestine problems it could have some relevance. In some lower developed countries this could help with some of the issues. They might not be able to afford the drugs that we have and if VesB does not cost a lot to make and the molecule does its job efficiently this could be of major use to the developing nations. | ||
== Structural highlights == | == Structural highlights == | ||
| - | + | This structure is a quaternary structure and the primary <scene name='79/799589/Secondary_structures/1'>Secondary Structures</scene> in VesB is beta sheets. In the molecule it has an alpha helix and some random coils spread around in the structure. The structure and how much space it takes up can be shown in the <scene name='79/799589/Vesb_spacefill/5'>Space-filling view</scene>. There are <scene name='79/799596/Domains/1'>two domains</scene> that make up VesB. The <scene name='79/799587/Active_site/1'>active site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221. It has a hydrophobic pocket that is made up of Val159, Val180, Ile164 and has a cleavage site made up of two amino acids Arg32, Ile33. | |
| - | + | ||
| - | <scene name='79/799587/Active_site/1'>active site</scene> | + | |
<scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> | <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> | ||
| + | <scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene> | ||
| + | == Kinetic Data == | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:13, 17 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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Structure of Vibrio cholerae protease B, VesB
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ 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
- ↑ 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
