User:Tilman Schirmer/Sandbox 203

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(References)
Current revision (14:45, 15 July 2009) (edit) (undo)
(PlzD in complex with c-di-GMP)
 
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<applet load='1yln.pdb' scene='User:Tilman_Schirmer/Sandbox_203/1yln_full/3' size='300' frame='true' align='right' caption='PlzD [[1yln]]' />
<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'>YcrR-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>
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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>
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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<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]]' />
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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), <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/4'>(blow-up)</scene>.
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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>.
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Zhang R, Zhou M, Moy S, Collart FR, Joachimiak A. 2005. The crystal structure of
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* Zhang R, Zhou M, Moy S, Collart FR, Joachimiak A. 2005. The crystal structure of
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the hypothetical protein vca0042 from Vibrio cholerae O1. Joint Center of Structural Genomics (JCSG).
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the hypothetical protein vca0042 from <i>Vibrio cholerae O1</i>. Midwest Center of Structural Genomics (MCSG).
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Current revision

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C-di-GMP receptors with PilZ domain

PlzD

PlzD 1yln

Drag the structure with the mouse to rotate

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

PlzD 2rde

Drag the structure with the mouse to rotate

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

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