C-di-GMP receptors with PilZ domain
From Proteopedia
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== PlzD == | == PlzD == | ||
| - | + | <applet load='1yln.pdb' scene='User:Tilman_Schirmer/Sandbox_203/1yln_full/3' size='300' frame='true' align='right' caption='PlzD [[1yln]]' /> | |
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<scene name='User:Tilman_Schirmer/Sandbox_203/1yln_full/2'>PlzD</scene> from <i>Vibrio cholerae</i> is composed of a <scene name='User:Tilman_Schirmer/Sandbox_203/Ycrr_n_domain/2'>YcgR-N*</scene> and a C-terminal <scene name='User:Tilman_Schirmer/Sandbox_203/Pilz_domain/2'>PilZ</scene> domain (with very similar fold). <br> <br> | <scene name='User:Tilman_Schirmer/Sandbox_203/1yln_full/2'>PlzD</scene> from <i>Vibrio cholerae</i> is composed of a <scene name='User:Tilman_Schirmer/Sandbox_203/Ycrr_n_domain/2'>YcgR-N*</scene> and a C-terminal <scene name='User:Tilman_Schirmer/Sandbox_203/Pilz_domain/2'>PilZ</scene> domain (with very similar fold). <br> <br> | ||
The c-di-GMP <scene name='User:Tilman_Schirmer/Sandbox_203/Active_site_global/6'>binding site</scene> is formed by arginine residues of the inter-domain linker and the PlzD domain surface <scene name='User:Tilman_Schirmer/Sandbox_203/Active_site_close/5'>(blow-up with labels)</scene>. | The c-di-GMP <scene name='User:Tilman_Schirmer/Sandbox_203/Active_site_global/6'>binding site</scene> is formed by arginine residues of the inter-domain linker and the PlzD domain surface <scene name='User:Tilman_Schirmer/Sandbox_203/Active_site_close/5'>(blow-up with labels)</scene>. | ||
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== PlzD in complex with c-di-GMP== | == PlzD in complex with c-di-GMP== | ||
| - | + | <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]]' /> | |
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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), see also <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/5'>blow-up</scene>. | 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), see also <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/5'>blow-up</scene>. | ||
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==References== | ==References== | ||
Current revision
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), see also .
References
PlzD structure 1yln:
- Zhang R, Zhou M, Moy S, Collart FR, Joachimiak A. 2005. The crystal structure of
the hypothetical protein vca0042 from Vibrio cholerae O1. Midwest Center of Structural Genomics (MCSG).
PlzD - c-di-GMP structure 2rde:
- Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta-Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF. The structural basis of cyclic diguanylate signal transduction by PilZ domains. EMBO J. 2007 Dec 12;26(24):5153-66. Epub 2007 Nov 22. PMID:18034161
