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'''The Subtilisin Domain:''' It contains ten helices (alpha 1 to 10) and twelve chains (beta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of Kex2 ([[1r64]]), which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> Asp78, His115, and Ser336 residues characteristic of subtilisins. In addition, four loops (L) protrude from the N-terminal subtilisin domain of ASP : Gly3– Pro26 (<scene name='82/829344/L1/2'>L1</scene>), Asn221–Phe241 (<scene name='82/829344/L2/2'>L2</scene>), Gly300–Cys326 (<scene name='82/829344/L3/2'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/2'>L4</scene>). L1, L2, and L3 have random coil structure, whereas L4 forms a hairpin that protrudes toward the P-domain. Moreover, two <scene name='82/829344/Disulfide_bridges/2'>disulfide bridges</scene> are formed between Cys4 and Cys24 in L1 and between Cys301 and Cys326 in L3, which stabilize those loops. | '''The Subtilisin Domain:''' It contains ten helices (alpha 1 to 10) and twelve chains (beta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of Kex2 ([[1r64]]), which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> Asp78, His115, and Ser336 residues characteristic of subtilisins. In addition, four loops (L) protrude from the N-terminal subtilisin domain of ASP : Gly3– Pro26 (<scene name='82/829344/L1/2'>L1</scene>), Asn221–Phe241 (<scene name='82/829344/L2/2'>L2</scene>), Gly300–Cys326 (<scene name='82/829344/L3/2'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/2'>L4</scene>). L1, L2, and L3 have random coil structure, whereas L4 forms a hairpin that protrudes toward the P-domain. Moreover, two <scene name='82/829344/Disulfide_bridges/2'>disulfide bridges</scene> are formed between Cys4 and Cys24 in L1 and between Cys301 and Cys326 in L3, which stabilize those loops. | ||
- | '''The P-domain:''' The core of the P-domain in ASP contains eight beta-strands (beta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/2'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/ | + | '''The P-domain:''' The core of the P-domain in ASP contains eight beta-strands (beta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/2'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/4'>pL1</scene>(Gly521–Thr525, beta 5, 6, and 12) and <scene name='82/829344/Pl2/4'>pL2</scene> (Gly557–Asn578, béta 25), and it is situated close to <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> Asp78,His115,and Ser336. |
All these domains are represented schematically in the article <ref>Structural Basis for the Kexin-like Serine Protease from Aeromonas sobria as Sepsis-causing Factor. H Kobayashi et al. J Biol Chem. 284(40): 27655–27663 (2009)</ref> : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F2/ '''representation 2D of ASP'''] | All these domains are represented schematically in the article <ref>Structural Basis for the Kexin-like Serine Protease from Aeromonas sobria as Sepsis-causing Factor. H Kobayashi et al. J Biol Chem. 284(40): 27655–27663 (2009)</ref> : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F2/ '''representation 2D of ASP'''] |
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The serine protease from Aeromonas sobria : ASP
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References
- ↑ 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
- ↑ Siezen RJ & Leunissen JAM (1997) Subtilase: the superfamily of subtilisin-like serine proteases. Protein Sci 6: 501–523.
- ↑ Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al. (2017)
- ↑ http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock
- ↑ Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)
- ↑ Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura T, Murakami Y, Nitta H. Biol. Chem. 398 1055-1068 (2017)
- ↑ Structural Basis for the Kexin-like Serine Protease from Aeromonas sobria as Sepsis-causing Factor. H Kobayashi et al. J Biol Chem. 284(40): 27655–27663 (2009)
- ↑ http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png
- ↑ Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura T, Murakami Y, Nitta H. Biol. Chem. 398 1055-1068 (2017)
- ↑ Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,
- ↑ Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al. Japan (2002)
- ↑ Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al. Japan (2002)
- ↑ Joseph, S. W., O. P. Daily, W. S. Hunt, R. J. Seidler, D. A. Allen, and R. R. Colwell. 1979. Aeromonas primary wound infection of a diver in polluted waters. J. Clin. Microbiol. 10:46-49.
- ↑ Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,
- ↑ Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin. Murakami Y et al. Biol Chem. 393(10):1193-200 (2012)