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User:Tilman Schirmer/Sandbox 204
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< User:Tilman Schirmer(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 | + | <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 | + | <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 ( | + | <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 | + | <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 | + | 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"/> | ||
Current revision
WspR
Overview
|
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 site
|
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.
References
WspR structure 3bre:
- 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
