User:Tilman Schirmer/Sandbox 201
From Proteopedia
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[[User:Tilman_Schirmer/Sandbox_200|back]]  | [[User:Tilman_Schirmer/Sandbox_200|back]]  | ||
| - | + | '''PleD'''  | |
| - | ===  | + | ===Overview===  | 
<applet load='1w25' scene='User:Tilman_Schirmer/Sandbox_201/Protomer/5' size='300' frame='true' align='right' caption='Diguanylate cyclase PleD (1w25)' />  | <applet load='1w25' scene='User:Tilman_Schirmer/Sandbox_201/Protomer/5' size='300' frame='true' align='right' caption='Diguanylate cyclase PleD (1w25)' />  | ||
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<br><br><br><br><br><br><br><br><br>  | <br><br><br><br><br><br><br><br><br>  | ||
| - | + | ===Substrate binding===  | |
| + | <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/4' size='300' frame='true' align='right' caption='Diguanylate cyclase PleD (2v0n)' />  | ||
| - | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/  | + | |
| + | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/5'>substrate binding site</scene> as identified in the structure of PleD  in complex with  <scene name='User:Tilman_Schirmer/Sandbox_201/Gtp-a-s/2'>GTP-alpha-S / Mg++</scene>. The GGDEFY domain binds only '''one''' GTP subsrate molecule. For the reaction to proceed, '''two''' GTP loaded GGDEF domains have to align antiparallely. MODEL.  | ||
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<br><br><br><br><br><br><br><br><br><br><br><br><br>  | <br><br><br><br><br><br><br><br><br><br><br><br><br>  | ||
| - | == Allosteric product binding site ==  | + | === Allosteric product binding site ===  | 
<applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/5gp/1' size='300' frame='true' align='right' caption='Allosteric product binding site' />  | <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/5gp/1' size='300' frame='true' align='right' caption='Allosteric product binding site' />  | ||
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<applet load='1w25' scene='User:Tilman_Schirmer/Sandbox_201/Loose_dimer/3' size='250' frame='true' align='left' caption='non-activated (1w25)' /> <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Tight_dimer/2' size='250' frame='true' align='center' caption='activated (BeF3- modified; 2v0n)' />  | <applet load='1w25' scene='User:Tilman_Schirmer/Sandbox_201/Loose_dimer/3' size='250' frame='true' align='left' caption='non-activated (1w25)' /> <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Tight_dimer/2' size='250' frame='true' align='center' caption='activated (BeF3- modified; 2v0n)' />  | ||
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| - | == Non-activated conformation ==  | ||
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| - | [[1w25]]   | ||
| - | <applet load='1w25' scene='User:Tilman_Schirmer/Sandbox_201/Protomer/2' size='300' frame='true' align='right' caption='1w25' />  | ||
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| - | <scene name='User:Tilman_Schirmer/Sandbox_201/Protomer/2'>Protomer</scene>: <scene name='User:Tilman_Schirmer/Sandbox_201/Rec/1'>Rec domain</scene>,  | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_201/Rec2/1'>Rec' domain</scene>, <scene name='User:Tilman_Schirmer/Sandbox_201/Ggdef/1'>GGDEF domain</scene>  | ||
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| - | <scene name='User:Tilman_Schirmer/Sandbox_201/Loose_dimer/2'>Loose dimer</scene>  | ||
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| - | <br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>  | ||
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| - | == Activated conformation ==  | ||
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| - | [[2v0n]]   | ||
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| - | <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Protomer_activeated/1' size='300' frame='true' align='right' caption='2v0n' />  | ||
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| - | <scene name='User:Tilman_Schirmer/Sandbox_201/Protomer_activeated/1'>Protomer</scene>  | ||
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| - | <scene name='User:Tilman_Schirmer/Sandbox_201/Tight_dimer/3'>Tight dimer</scene>  | ||
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| - | <br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>  | ||
Current revision
PleD
Contents | 
Overview
  | 
 from Caulobacter crescentus is a response regulator with an unorthodox catalytic, diguanylate cyclase, output domain. It is composed of a canonical CheY-like response regulator receiver () domain, 
a Rec-like () adaptor domain, 
and a C-terminal  domain that confers the catalytic acitvity.
The GGDEF domain is named after the highly conserved  (in PleD it is GGEEF) that locates to a β-hairpin.
Substrate binding
  | 
The motif is part of the  as identified in the structure of PleD  in complex with  . The GGDEFY domain binds only one GTP subsrate molecule. For the reaction to proceed, two GTP loaded GGDEF domains have to align antiparallely. MODEL.
Allosteric product binding site
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C-di-GMP
Primary inhibition site (Ip)
Secondary inhibition site (Is)
Primary and secondary inhibition sites
Two conformations
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