This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
User:Tilman Schirmer/Sandbox 204
From Proteopedia
(→Allosteric product binding site) |
(→Allosteric product binding site) |
||
| Line 22: | Line 22: | ||
== Allosteric product binding site == | == Allosteric product binding site == | ||
| - | <applet load='2bre' scene='User:Tilman_Schirmer/Sandbox_204/Ip/ | + | <applet load='2bre' scene='User:Tilman_Schirmer/Sandbox_204/Ip/3' size='300' frame='true' align='right' caption='WspR ([[3bre]])' /> |
| - | There are two allosteric sites (<scene name='User:Tilman_Schirmer/Sandbox_204/Ip/ | + | There are two allosteric sites (<scene name='User:Tilman_Schirmer/Sandbox_204/Ip/3'>primary inhibition site, Ip,</scene> and <scene name='User:Tilman_Schirmer/Sandbox_204/Is/3'>secondary inhibition site, Is,</scene>) that are cross-linked by <scene name='User:Tilman_Schirmer/Sandbox_204/C-di-gmp_dimer/1'>(c-di-GMP)2</scene> dimers in the <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/5'>tetrameric</scene> molecule. For a close-up click <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/4'>here</scene>. |
<scene name='User:Tilman_Schirmer/Sandbox_204/Prim_sec_inhibition_site_c2e/1'>Primary and secondary inhibition sites + C2E</scene> | <scene name='User:Tilman_Schirmer/Sandbox_204/Prim_sec_inhibition_site_c2e/1'>Primary and secondary inhibition sites + C2E</scene> | ||
<br><br><br><br> | <br><br><br><br> | ||
Revision as of 15:58, 1 July 2009
WspR
Overview
|
: ,
from Pseudomonas aeruginosa is a response regulator with an unorthodox catalytic, diguanylate cyclase, output domain. It is composed of a canonical CheY-like response regulator receiver () domain and a C-terminal domain that confers the catalytic acitvity.
Although not modified (e.g. phosphorylated) at the active Asp (Asp70), the Rec domains mediate formation of WspR. Two dimers, in turn, are associated by head-to-head contact to a of approximate 222 (D2) symmetry.
i
Allosteric product binding site
|
There are two allosteric sites ( and ) that are cross-linked by dimers in the molecule. For a close-up click .
