User:Tilman Schirmer/Sandbox 204: Difference between revisions
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Overview
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> 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>). | 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>). Note that there are four (c-di-GMP)<sub>2</sub> dimers per WspR tetramer. | ||
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Revision as of 19:16, 1 July 2009
WspR
OverviewOverview
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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 (i.e. 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 siteAllosteric 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 (, , ). Note that there are four (c-di-GMP)2 dimers per WspR tetramer.