User:Tilman Schirmer/Sandbox 211
From Proteopedia
(→Complete active site formed by GGDEF dimer) |
(→Substrate binding) |
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| - | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/4'>substrate binding site</scene> as identified in the structure of PleD in complex with <scene name='User:Tilman_Schirmer/Sandbox_201/Gtp-a-s/1'>GTP-alpha-S / Mg++</scene>. The GGDEFY domain binds only '''one''' GTP subsrate molecule. For the reaction to proceed, '''two''' GTP loaded GGDEF domains have to align antiparallely | + | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/4'>substrate binding site</scene> as identified in the structure of PleD in complex with <scene name='User:Tilman_Schirmer/Sandbox_201/Gtp-a-s/1'>GTP-alpha-S/Mg<sup>++</sup></scene>. The GGDEFY domain binds only '''one''' GTP subsrate molecule. For the reaction to proceed, '''two''' GTP loaded GGDEF domains have to align antiparallely. |
Revision as of 11:06, 21 June 2009
Overview
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from Caulobacter crescentus is a response regulator with an unorthodox catalytic, diguanylate cyclase, output domain. It is composed of a canonical CheY-like response regulator receiver () domain,
a Rec-like () adaptor domain,
and a C-terminal domain that confers the catalytic acitvity.
The GGDEF domain is named after the highly conserved (in PleD it is GGEEF) that locates to a β-hairpin.
Substrate binding
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The motif is part of the as identified in the structure of PleD in complex with . The GGDEFY domain binds only one GTP subsrate molecule. For the reaction to proceed, two GTP loaded GGDEF domains have to align antiparallely.
Complete active site
After binding of the it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (, ).
