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
VesB activity was measured with different concentrations of Boc-Gln-Ala-Arg-7-amino-4-AMC in 5 mM HEPES, pH 7.5, at 37 °C. B, purified VesB (0.08 �g/ml) was incubated with 50 �M leupeptin, 1 mM benzamidine, or 10 mM EDTA for 10 min at 37 °C. The Boc-Gln-AlaArg-7-amino-4-AMC (0.05 mM final concentration) was added and VesB activity was measured. When Boc-Gln-AlaArg-7-amino-4-AMC increases so does the pmol/min.
