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User:Tilman Schirmer/Sandbox 204
From Proteopedia
(→Allosteric product binding site) |
(→Allosteric product binding site) |
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<applet load='2bre' scene='User:Tilman_Schirmer/Sandbox_204/Ip/3' size='300' frame='true' align='right' caption='WspR ([[3bre]])' /> | <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/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 (c-di-GMP)<sub>2</sub> | + | 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 (c-di-GMP)<sub>2</sub> 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/Tetramer/6'>Ip-site</scene>, <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/8'>Is-site</scene>, <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/9'>c-di-GMP dimer</scene>). |
<br><br><br><br> | <br><br><br><br> | ||
Revision as of 16:08, 1 July 2009
WspR
Overview
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: ,
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
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There are two allosteric sites ( and ) that are cross-linked by (c-di-GMP)2 dimers in the molecule. For a close-up click (, , ).
