Sandbox Reserved 1091: Difference between revisions

Line 29:

== Domains ==

'''The Subtilisin Domain:''' It contains 10 helices (alpha 1 to 10) and twelve chains (béta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of ''Kex2'', which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78, His-115, and Ser-336 residues characteristic of subtilisins. In addition, 4 loops (L) protrude from the N-terminal subtilisin domain of ASP: Gly-3– Pro-26 (<scene name='82/829344/L1/1'>L1</scene>), Asn-221–Phe-241 (<scene name='82/829344/L2/1'>L2</scene>), Gly-300–Cys-326 (<scene name='82/829344/L3/1'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/1'>L4</scene>). L1, L2, and L3 have random coil structure, whereas L4 forms a hairpin that protrudes toward the P-domain. Moreover, two disulfide bridges are formed between Cys-4 and Cys-24 in L1 and between Cys-301 and Cys-326 in L3, which stabilize those loops.

'''The Subtilisin Domain:''' It contains 10 helices (alpha 1 to 10) and twelve chains (béta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of ''Kex2'', which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78, His-115, and Ser-336 residues characteristic of subtilisins. In addition, 4 loops (L) protrude from the N-terminal subtilisin domain of ASP: Gly-3– Pro-26 (<scene name='82/829344/L1/1'>L1</scene>), Asn-221–Phe-241 (<scene name='82/829344/L2/1'>L2</scene>), Gly-300–Cys-326 (<scene name='82/829344/L3/1'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/1'>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/1'>disulfide bridges</scene> are formed between Cys-4 and Cys-24 in L1 and between Cys-301 and Cys-326 in L3, which stabilize those loops.

'''The P-domain:''' The core of the P-domain in ASP contains 8 béta-strands (béta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/1'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/1'>pL1</scene>(Gly 521–Thr 525, béta 5, 6, and 12) and <scene name='82/829344/Pl2/1'>pL2</scene> (Gly-557–Asn-578, béta 25), and it is situated close to <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78,His-115,and Ser-336.

Sandbox Reserved 1091: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 29: / Line 29: @@
 == Domains ==
-'''The Subtilisin Domain:''' It contains 10 helices (alpha 1 to 10) and twelve chains (béta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of ''Kex2'', which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78, His-115, and Ser-336 residues characteristic of subtilisins. In addition, 4 loops (L) protrude from the N-terminal subtilisin domain of ASP: Gly-3– Pro-26 (<scene name='82/829344/L1/1'>L1</scene>), Asn-221–Phe-241 (<scene name='82/829344/L2/1'>L2</scene>), Gly-300–Cys-326 (<scene name='82/829344/L3/1'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/1'>L4</scene>). L1, L2, and L3 have random coil structure, whereas L4 forms a hairpin that protrudes toward the P-domain. Moreover, two disulfide bridges are formed between Cys-4 and Cys-24 in L1 and between Cys-301 and Cys-326 in L3, which stabilize those loops.
+'''The Subtilisin Domain:''' It contains 10 helices (alpha 1 to 10) and twelve chains (béta 1 to 10 and béta 13 to 14). The N-terminal domain of ASP seems to be like the catalytic domain of ''Kex2'', which is similar to those of subtilisin and other subtilisin-related proteases. This ASP catalytic site contains <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78, His-115, and Ser-336 residues characteristic of subtilisins. In addition, 4 loops (L) protrude from the N-terminal subtilisin domain of ASP: Gly-3– Pro-26 (<scene name='82/829344/L1/1'>L1</scene>), Asn-221–Phe-241 (<scene name='82/829344/L2/1'>L2</scene>), Gly-300–Cys-326 (<scene name='82/829344/L3/1'>L3</scene>), and Gln-377–Glu-397 (<scene name='82/829344/L4/1'>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/1'>disulfide bridges</scene> are formed between Cys-4 and Cys-24 in L1 and between Cys-301 and Cys-326 in L3, which stabilize those loops.
 '''The P-domain:''' The core of the P-domain in ASP contains 8 béta-strands (béta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/1'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/1'>pL1</scene>(Gly 521–Thr 525, béta 5, 6, and 12) and <scene name='82/829344/Pl2/1'>pL2</scene> (Gly-557–Asn-578,  béta 25), and it is situated close to <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> Asp-78,His-115,and Ser-336.