User:Tilman Schirmer/Sandbox 204
From Proteopedia
< User:Tilman Schirmer(Difference between revisions)
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| - | <br>Although not modified (i.e. phosphorylated) at the active Asp (<scene name='User:Tilman_Schirmer/Sandbox_204/Rec/ | + | <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. |
Current revision
WspR
Overview
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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
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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
