User:Tilman Schirmer/Sandbox 202
From Proteopedia
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<scene name='User:Tilman_Schirmer/Sandbox_202/Yuki_dimer/3'>YukI</scene> is a dimer with each protomer composed of an <scene name='User:Tilman_Schirmer/Sandbox_202/Eal_domain/1'>EAL domain</scene>, a long <scene name='User:Tilman_Schirmer/Sandbox_202/Connection/1'>helical linker</scene>, and a <scene name='User:Tilman_Schirmer/Sandbox_202/Pas_like_domain/1'>PAS-like domain</scene>. <br> | <scene name='User:Tilman_Schirmer/Sandbox_202/Yuki_dimer/3'>YukI</scene> is a dimer with each protomer composed of an <scene name='User:Tilman_Schirmer/Sandbox_202/Eal_domain/1'>EAL domain</scene>, a long <scene name='User:Tilman_Schirmer/Sandbox_202/Connection/1'>helical linker</scene>, and a <scene name='User:Tilman_Schirmer/Sandbox_202/Pas_like_domain/1'>PAS-like domain</scene>. <br> | ||
| - | The <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>active site </scene> is situated at the C-terminal end of the central β-barrel of the EAL domain (with TIM fold). The residues of the <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close_labels/1'> | + | The <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>active site </scene> is situated at the C-terminal end of the central β-barrel of the EAL domain (with TIM fold). The residues of the active site <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close_labels/1'>(here shown with labels)</scene> are well conserved, including E33 and L35 of the EAL signature motif. <br> |
| + | The <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_ligand/3'>c-di-GMP substrate</scene> is bound flat upon the actve site with the divalent metal (here Ca<sup>++</sup> being sandwiched between binding site and c-di-GMP. | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_202/ | + | <br><br><br><br><br><br> |
| - | + | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>Active site (Q19, E33, L35, R37, N88, E122, P152, K173, Q209)</scene> | |
<scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_ligand/3'>Active site + ligand + Ca++</scene> | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_ligand/3'>Active site + ligand + Ca++</scene> | ||
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| - | <br><br><br><br><br><br><br><br><br> | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>Active site (Q19, E33, L35, R37, N88, E122, P152, K173, Q209)</scene> | ||
== BlrP1 == | == BlrP1 == | ||
Revision as of 20:54, 30 June 2009
C-di-GMP specific phosphodiesterases
YukI
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is a dimer with each protomer composed of an , a long , and a .
The is situated at the C-terminal end of the central β-barrel of the EAL domain (with TIM fold). The residues of the active site are well conserved, including E33 and L35 of the EAL signature motif.
The is bound flat upon the actve site with the divalent metal (here Ca++ being sandwiched between binding site and c-di-GMP.
BlrP1
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