Sandbox Reserved 1461

From Proteopedia

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Revision as of 21:35, 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

1 Function
2 Disease
3 Relevance
4 Structural highlights
5 Kinetic Data

Function

The organism in which the protein can be found in is ibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). Its biological role has yet to be determined, VesB is produced both in vitro and in vivo. It has had detection in laboratory-grown culter. VesB ^[1]is most likely produced as a zymogen because sequene alignment with trypsinogen identified a putative cleavage site for activation and a catalytic triad, His-Asp-Ser. VesB efficiently cleaved a trypsin substrate but not chymotrypsin and elastase substrates.

Disease

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

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

This structure is a quaternary structure and the primary 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 . There are that make up VesB. VesB has has two in it domains. This molecule is and does not react well with water. The hydrophobic are important because they sow the area where the active site is located. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The 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.

Kinetic Data

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_1461"

@@ Line 13: / Line 13: @@
 == 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.
+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. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene>in it domains. This molecule is <scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene> and does not react well with water. The hydrophobic are important because they sow the area where the active site is located. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. 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='79/799596/Disulfide_bonds/1'>disulfide bonds</scene>
-<scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene>
 == Kinetic Data ==

Sandbox Reserved 1461

From Proteopedia

Revision as of 21:35, 17 November 2018

Structure of Vibrio cholerae protease B, VesB

Contents

Function

Disease

Relevance

Structural highlights

Kinetic Data

References

Views

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