Sandbox Reserved 1091: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
The ''Aeromonas Sobria Serine Protease'' ASP protein is a '''serine protease''' that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of ''Kex2'' <ref>PMID:2646633</ref> ([[1r64]]), a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site. | The ''Aeromonas Sobria Serine Protease'' ASP protein is a '''serine protease''' that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of ''Kex2'' <ref>PMID:2646633</ref> ([[1r64]]), a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site. | ||
This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal septic shock. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multivisceral failure, including the lungs, kidneys and liver, can be observed. <ref> | This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal septic shock [https://www.msdmanuals.com Septic shock]. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multivisceral failure, including the lungs, kidneys and liver, can be observed. <ref>https://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref> | ||
ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunction like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.m.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally it can causes the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''. | ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunction like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.m.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally it can causes the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''. | ||
| Line 24: | Line 24: | ||
The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>. | The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>. | ||
Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, and <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to ''Kex2'', ASP contains no Ca2+ binding sites near its catalytic site. Those Ca2+ binding Site are important because ... | Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, and <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to ''Kex2'', ASP contains no Ca2+ binding sites near its catalytic site. | ||
Those Ca2+ binding Site are important because ... | |||
| Line 40: | Line 42: | ||
'''Mechanism:''' The mechanism is the following: The histidine will react with the serine and deprotonate it. '''The deprotonated hydroxyl group of the serine will act as a nucleophilic species''' and attack the carbon from the carbonyl function on the peptide. This will lead to the formation of a tetrahedral intermediate. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | '''Mechanism:''' The mechanism is the following: The histidine will react with the serine and deprotonate it. '''The deprotonated hydroxyl group of the serine will act as a nucleophilic species''' and attack the carbon from the carbonyl function on the peptide. This will lead to the formation of a tetrahedral intermediate. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | ||
