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User:Tilman Schirmer/Sandbox 204
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<applet load='2bre' scene='User:Tilman_Schirmer/Sandbox_204/Protomer/3' size='300' frame='true' align='right' caption='WspR ([[3bre]])' /> | <applet load='2bre' scene='User:Tilman_Schirmer/Sandbox_204/Protomer/3' size='300' frame='true' align='right' caption='WspR ([[3bre]])' /> | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_204/Protomer/3'>WspR </scene> 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 (<scene name='User:Tilman_Schirmer/Sandbox_204/Rec/2'>Rec</scene>) and a C-terminal <scene name='User:Tilman_Schirmer/Sandbox_204/Ggdef/2'>catalytic GGDEF domain</scene> domain that confers the catalytic activity with all canonical <scene name='User:Tilman_Schirmer/Sandbox_204/ | + | <scene name='User:Tilman_Schirmer/Sandbox_204/Protomer/3'>WspR </scene> 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 (<scene name='User:Tilman_Schirmer/Sandbox_204/Rec/2'>Rec</scene>) and a C-terminal <scene name='User:Tilman_Schirmer/Sandbox_204/Ggdef/2'>catalytic GGDEF domain</scene> domain that confers the catalytic activity with all canonical <scene name='User:Tilman_Schirmer/Sandbox_204/Substrate binding site/2'>active site residues</scene> present. |
Revision as of 16:13, 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 activity with all canonical present.
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.
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 (, , ).
