User:Tilman Schirmer/Sandbox 211
From Proteopedia
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| - | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/5'>substrate binding site</scene> as identified in the structure of PleD in complex with <scene name='User:Tilman_Schirmer/Sandbox_201/Gtp-a-s/2'>GTP-alpha-S/Mg | + | The motif is part of the <scene name='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/5'>substrate binding site</scene> as identified in the structure of PleD in complex with <scene name='User:Tilman_Schirmer/Sandbox_201/Gtp-a-s/2'>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. |
Revision as of 13:08, 21 June 2009
PleD
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
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After binding of the it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (, ). Then, by inter-molecular nucleophilic in-line attack of the O3' atom onto the α-phosphorous of the other GTP substrate molecule two phosphodiester bonds are formed and 2 pyrophosphate molecules are released.
