Sandbox Reserved 1461 - Revision history

Nicholas Kelly at 19:59, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:59:21 GMT

←Older revision		Revision as of 19:59, 3 December 2018
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	== 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. This molecule is <scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene> and does not react well with water. The hydrophobic view is important because they show the area where the active site is located it is labeled in purple. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The <scene name='79/799589/Active_site/4'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, blue, and green. The other amino acids that are found in the active site are highlighted black. 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. This molecule is <scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene> and does not react well with water. The hydrophobic view is important because they show the area where the active site is located it is labeled in purple. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The active site will easily hydrogen bond showing that it is hydrophobic. The <scene name='79/799589/Active_site/4'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, blue, and green. The other amino acids that are found in the active site are highlighted black. 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.

Nicholas Kelly at 19:52, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:52:28 GMT

←Older revision		Revision as of 19:52, 3 December 2018
Line 19:		Line 19:
	== 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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 show the area where the active site is located it is labeled in purple. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The <scene name='79/799589/Active_site/4'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, blue, and green. The other amino acids that are found in the active site are highlighted black. 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. This molecule is <scene name='79/799589/Hydrophobic_and_polar/1'>Hydrophobic</scene> and does not react well with water. The hydrophobic view is important because they show the area where the active site is located it is labeled in purple. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The <scene name='79/799589/Active_site/4'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, blue, and green. The other amino acids that are found in the active site are highlighted black. 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.

Nicholas Kelly at 19:51, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:51:20 GMT

←Older revision		Revision as of 19:51, 3 December 2018
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	== Kinetic Data ==		== 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 50M 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. <ref>PMID: 24459146</ref><ref> ~~https~~:~~//www.ebi.ac.uk/interpro/potm/2005_9/Page1.htm</ref><ref>http://www.jbc.org/content/286/19/16555</ref><ref>http://www.jbc.org/content/289/12/8288~~</ref>	+	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 50M 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. <ref>PMID: 24459146</ref><ref> PMID: 21385872</ref>
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Nicholas Kelly at 19:48, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:48:37 GMT

←Older revision		Revision as of 19:48, 3 December 2018
Line 23:		Line 23:

	== Kinetic Data ==		== 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 50M 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. <ref>~~https~~://s3.us-east-1.amazonaws.com/learn-us-east-1-prod-fleet01-xythos/5b158bd279e57/488299?response-content-disposition=inline%3B%20filename%2A%3DUTF-8%27%27J.%2520Biol.%2520Chem.-2014-Gadwal-8288-98%2520Vibrio%2520cholerae%2520serine%2520protease.pdf&response-content-type=application%2Fpdf&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20181116T020506Z&X-Amz-SignedHeaders=host&X-Amz-Expires=21600&X-Amz-Credential=AKIAIBGJ7RCS23L3LEJQ%2F20181116%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=9e1220b65465ef522a3848949b1858eade9275dd28253481cb14469e6915e30c</ref><ref> https://www.ebi.ac.uk/interpro/potm/2005_9/Page1.htm</ref><ref>http://www.jbc.org/content/286/19/16555</ref><ref>http://www.jbc.org/content/289/12/8288</ref>	+	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 50M 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. <ref>PMID: 24459146</ref><ref> https://www.ebi.ac.uk/interpro/potm/2005_9/Page1.htm</ref><ref>http://www.jbc.org/content/286/19/16555</ref><ref>http://www.jbc.org/content/289/12/8288</ref>
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Nicholas Kelly at 19:06, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:06:26 GMT

←Older revision		Revision as of 19:06, 3 December 2018
Line 5:		Line 5:

	== Function ==		== Function ==
-	VesB, a serene protease found in the bacterium Vibrio cholerae, plays an important role in pathogenesis and intestine growth. VesB’s function is cleaving A subunit of cholera toxin, which helps in the activation of itself. The protease’s substrate may consist of a protein with arginine (XXRXX) and the products (XXR+XX).	+	<scene name='79/799589/Cartoon_vesb/2'>VesB</scene>, a serene protease found in the bacterium Vibrio cholerae, plays an important role in pathogenesis and intestine growth. VesB’s function is cleaving A subunit of cholera toxin, which helps in the activation of itself. The protease’s substrate may consist of a protein with arginine (XXRXX) and the products (XXR+XX).
	== Disease ==		== Disease ==
	Cholera, caused by Vibrio cholerae, is an infectious intestinal disease well known for its severe symptoms of diarrhea and cramps, which often results in death. The first sign of whether or not an individual has contracted the disease is the quick onset of diarrhea increasing in intensity over time. Secondary symptoms include vomiting, extreme thirst, abdominal cramps, and a blue-gray coloring. Lastly, the blood would thicken due to loss of fluid.		Cholera, caused by Vibrio cholerae, is an infectious intestinal disease well known for its severe symptoms of diarrhea and cramps, which often results in death. The first sign of whether or not an individual has contracted the disease is the quick onset of diarrhea increasing in intensity over time. Secondary symptoms include vomiting, extreme thirst, abdominal cramps, and a blue-gray coloring. Lastly, the blood would thicken due to loss of fluid.

Nicholas Kelly at 19:05, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 19:05:10 GMT

←Older revision		Revision as of 19:05, 3 December 2018
Line 19:		Line 19:
	== 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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 show 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='79/799589/Active_site/3'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, ~~magenta~~, and ~~pink~~. 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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 show the area where the active site is located it is labeled in purple. Being hydrophilic shows that it does mix well with water. They are both shown throughout the molecule. The <scene name='79/799589/Active_site/4'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, blue, and green. The other amino acids that are found in the active site are highlighted black. 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.

Nicholas Kelly at 17:04, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 17:04:19 GMT

←Older revision		Revision as of 17:04, 3 December 2018
Line 19:		Line 19:
	== 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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='79/799589/Active_site/3'>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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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 show 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='79/799589/Active_site/3'>Active Site</scene> of the molecule is made up of 3 amino acids. The amino acids are Asp125-His78-Ser221 which are highlighted in red, magenta, and pink. 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 ==		== 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 50M 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. <ref>https://s3.us-east-1.amazonaws.com/learn-us-east-1-prod-fleet01-xythos/5b158bd279e57/488299?response-content-disposition=inline%3B%20filename%2A%3DUTF-8%27%27J.%2520Biol.%2520Chem.-2014-Gadwal-8288-98%2520Vibrio%2520cholerae%2520serine%2520protease.pdf&response-content-type=application%2Fpdf&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20181116T020506Z&X-Amz-SignedHeaders=host&X-Amz-Expires=21600&X-Amz-Credential=AKIAIBGJ7RCS23L3LEJQ%2F20181116%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=9e1220b65465ef522a3848949b1858eade9275dd28253481cb14469e6915e30c</ref>	+	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 50M 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. <ref>https://s3.us-east-1.amazonaws.com/learn-us-east-1-prod-fleet01-xythos/5b158bd279e57/488299?response-content-disposition=inline%3B%20filename%2A%3DUTF-8%27%27J.%2520Biol.%2520Chem.-2014-Gadwal-8288-98%2520Vibrio%2520cholerae%2520serine%2520protease.pdf&response-content-type=application%2Fpdf&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20181116T020506Z&X-Amz-SignedHeaders=host&X-Amz-Expires=21600&X-Amz-Credential=AKIAIBGJ7RCS23L3LEJQ%2F20181116%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=9e1220b65465ef522a3848949b1858eade9275dd28253481cb14469e6915e30c</ref><ref> https://www.ebi.ac.uk/interpro/potm/2005_9/Page1.htm</ref><ref>http://www.jbc.org/content/286/19/16555</ref><ref>http://www.jbc.org/content/289/12/8288</ref>
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Nicholas Kelly at 16:21, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 16:21:53 GMT

←Older revision		Revision as of 16:21, 3 December 2018
Line 19:		Line 19:
	== 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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/~~Vesb_spacefil_final1~~/1'>~~Spacefill~~</scene>view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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='79/799589/Active_site/3'>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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefill/6'>spacefill</scene> view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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='79/799589/Active_site/3'>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.

Nicholas Kelly at 16:15, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 16:15:40 GMT

←Older revision		Revision as of 16:15, 3 December 2018
Line 19:		Line 19:
	== 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 two domains that make up VesB~~. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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='79/799589/Active_site/3'>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. VesB is made up of two different domains, it can be shown in this <scene name='79/799589/Vesb_spacefil_final1/1'>Spacefill</scene>view. VesB has has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> in it domains. The two different type of domains are the N-terminal and C-terminal domain. 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='79/799589/Active_site/3'>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.

Nicholas Kelly at 02:44, 3 December 2018

Nicholas Kelly — Mon, 03 Dec 2018 02:44:03 GMT

←Older revision		Revision as of 02:44, 3 December 2018
Line 5:		Line 5:

	== Function ==		== 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 <ref>PMID:24459146</ref>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~~.	+	VesB, a serene protease found in the bacterium Vibrio cholerae, plays an important role in pathogenesis and intestine growth. VesB’s function is cleaving A subunit of cholera toxin, which helps in the activation of itself. The protease’s substrate may consist of a protein with arginine (XXRXX) and the products (XXR+XX).
	== Disease ==		== 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~~.	+	Cholera, caused by Vibrio cholerae, is an infectious intestinal disease well known for its severe symptoms of diarrhea and cramps, which often results in death. The first sign of whether or not an individual has contracted the disease is the quick onset of diarrhea increasing in intensity over time. Secondary symptoms include vomiting, extreme thirst, abdominal cramps, and a blue-gray coloring. Lastly, the blood would thicken due to loss of fluid.
		+
		+	Cholera toxin, a byproduct of Vibrio cholerae, decreases the amount of fluid in the intestines. The toxin is produced by the CTXf bacteriophage residing subunit. The A subunit consists of an A1 domain containing the enzymatic active site and it assembles into a pentameric ring surrounding a central pore.
		+
	== 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~~.	+	Cholera has been recorded in early Sanskrit writings and has been a prevalent disease on the Indian subcontinent for years. In the 19th century, cholera spread across Europe and eventually advanced to North and South America. Today it continues to be a serious health issue in Africa, Asia, and Latin America.
		+
		+	There are as many as 200,000-500,000 cases per year and the mortality rates can reach as high as 20-50%. There are currently no effective prophylactics and treatment by rehydration often does not work because of the lack of clean water supplies. Research currently aims at targeting the cholera toxin itself, focusing specifically on the inhibition of its binding to receptors in the intestine and the development of anti-secretory agents.
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	== Structural highlights ==		== Structural highlights ==