User:Tilman Schirmer/Sandbox 204: Difference between revisions

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== Overview ==
== Overview ==


<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/Substrate_binding_site/2'>active site residues</scene> present.
<scene name='User:Tilman_Schirmer/Sandbox_204/Protomer/3'>WspR </scene> from ''Pseudomonas aeruginosa'' is a response regulator with an 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.




<br>Although not modified (i.e. phosphorylated) at the active Asp (Asp70), the Rec domains mediate formation of <scene name='User:Tilman_Schirmer/Sandbox_204/Dimer/1'>dimeric </scene> WspR. Two dimers, in turn, are associated by head-to-head contact to a <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/1'>tetramer</scene> of approximate 222 (D2) symmetry.  
<br>Although not modified (i.e. phosphorylated) at the active Asp (<scene name='User:Tilman_Schirmer/Sandbox_204/Rec/4'>Asp70</scene>), the Rec domains mediate formation of <scene name='User:Tilman_Schirmer/Sandbox_204/Dimer/1'>dimeric </scene> WspR. Two dimers, in turn, are associated by head-to-head contact to a <scene name='User:Tilman_Schirmer/Sandbox_204/Tetramer/1'>tetramer</scene> of approximate 222 (D2) symmetry.  




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== Allosteric product binding site ==
== Allosteric product binding site ==
<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 become 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)2</scene>). Note that there are four (c-di-GMP)<sub>2</sub> dimers per WspR tetramer.




<br><br><br><br>
<br><br><br><br>
==References==
WspR structure [[3bre]]:
<ref group="xtra">PMID:18366254</ref>
<references group="xtra"/>

Latest revision as of 17:55, 15 July 2009

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WspR

OverviewOverview

WspR 3bre

Drag the structure with the mouse to rotate

from Pseudomonas aeruginosa is a response regulator with an 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 (), 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

WspR 3bre

Drag the structure with the mouse to rotate

There are two allosteric sites ( and ) that become 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.






ReferencesReferences

WspR structure 3bre: [xtra 1]

  1. ↑ De N, Pirruccello M, Krasteva PV, Bae N, Raghavan RV, Sondermann H. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS Biol. 2008 Mar 25;6(3):e67. PMID:18366254 doi:10.1371/journal.pbio.0060067
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