Sandbox Reserved 1091: Difference between revisions
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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'''] | ||
