User:Tilman Schirmer/Sandbox 203
From Proteopedia
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<applet load='2rde.pdb' scene='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/3' size='300' frame='true' align='right' caption='PlzD [[2rde]]' /> | <applet load='2rde.pdb' scene='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/3' size='300' frame='true' align='right' caption='PlzD [[2rde]]' /> | ||
| - | Upon complex formation the relative domain arrangement is <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/3'>drastically changed</scene> (compare with [[1yln]] above). | + | Upon complex formation the relative domain arrangement is <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/3'>drastically changed</scene> (compare with [[1yln]] above), <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/4'>(blow-up)</scene>. |
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Revision as of 09:25, 15 July 2009
C-di-GMP receptors with PilZ domain
PlzD
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from Vibrio cholerae is composed of a and a C-terminal domain (with very similar fold).
The c-di-GMP is formed by arginine residues of the inter-domain linker and the PlzD domain surface .
PlzD in complex with c-di-GMP
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Upon complex formation the relative domain arrangement is (compare with 1yln above), .
