User:Tilman Schirmer/Sandbox 211
From Proteopedia
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After binding of the <scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/6'>GTP substrate</scene> it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (<scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/3'>view1</scene>, <scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/1'>view2</scene>). | After binding of the <scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/6'>GTP substrate</scene> it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (<scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/3'>view1</scene>, <scene name='User:Tilman_Schirmer/Sandbox_211/Competent_ggdef_dimer/1'>view2</scene>). | ||
Revision as of 12:42, 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
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After binding of the it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (, ).
