This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


User:Tilman Schirmer/Sandbox 204

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 45: Line 45:
<scene name='User:Tilman_Schirmer/Sandbox_204/Prim_sec_inhibition_site_c2e/1'>Primary and secondary inhibition sites + C2E</scene>
<scene name='User:Tilman_Schirmer/Sandbox_204/Prim_sec_inhibition_site_c2e/1'>Primary and secondary inhibition sites + C2E</scene>
<br><br><br><br>
<br><br><br><br>
- 
-
== Two conformations ==
 
- 
- 
- 
-
== Non-activated conformation ==
 
- 
- 
-
<br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>
 
- 
- 
- 
- 
-
== Activated conformation ==
 
- 
- 
- 
-
<br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>
 

Revision as of 20:37, 30 June 2009

back

WspR

Contents

Overview

WspR (3bre)

Drag the structure with the mouse to rotate

: ,

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 acitvity.




Although not modified (e.g. phosphorylated) at the active Asp (Asp70), WspR is found in the form with the contact mediated by the Rec domains.










Allosteric product binding site

WspR (3bre)

Drag the structure with the mouse to rotate


Primary inhibition site (Ip)


Secondary inhibition site (Is)

Is this correct?


Allosteric binding of the product c-di-GMP

C-di-GMP binding to the inhbition sites cross-links two dimers.





Proteopedia Page Contributors and Editors (what is this?)

Tilman Schirmer

Personal tools