Sandbox Reserved 1091

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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 (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, 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 (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.
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Thos protein is secreted by the Anaerobic bacterium Aeromonas Sobria, which can cause potentially lethal septic shock. Sepsis [http://www.mdsmanuals.com Septic Shock] is
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Thos protein is secreted by the Anaerobic bacterium Aeromonas Sobria, which can cause potentially lethal septic shock. [http://www.mdsmanuals.com Septic Shock] 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.
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ASP is a sepsis-related factor. It can cause several dysfunction like by inducing vascular leakage, reducing blood pressure via the activation of the kinin system or promoting human plasma coagulation through the activation of prothrombin. Finally it can causes the formation of pus and edema through the action of anaphylatoxin C5a [[4p3a]]. ASP mediates in fact the induction of disseminated intravascular coagulation through alpha-thrombin production, which is a common and deadly consequence of sepsis”. Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with A. sobria.
The maturation of ASP is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain a propeptide (such as Kex2) that is involved in the proper folding of the protein.
The maturation of ASP is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain a propeptide (such as Kex2) that is involved in the proper folding of the protein.

Revision as of 17:11, 11 January 2020

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
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The serine protease from Aeromonas sobria

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References

  1. Fuller RS, Brake A, Thorner J. Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. Proc Natl Acad Sci U S A. 1989 Mar;86(5):1434-8. PMID:2646633
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