User:Tilman Schirmer/Sandbox 203

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C-di-GMP receptors with PilZ domain

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 .

Upon complex formation the relative domain arrangement is (compare with 1yln above), see also .

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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 <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), see also <scene name='User:Tilman_Schirmer/Sandbox_203/Plzd_active_site_monomer_ligan/4'>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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