User:Tilman Schirmer/Sandbox 211

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(Substrate binding)
(Substrate binding)
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===Substrate binding===
===Substrate binding===
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<applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/4' size='300' frame='true' align='right' caption='Diguanylate cyclase PleD (2v0n)' />
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<applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_201/Substrate_binding_site/5' size='300' frame='true' align='right' caption='Diguanylate cyclase PleD (2v0n)' />

Revision as of 11:14, 21 June 2009

Overview

Diguanylate cyclase PleD (1w25)

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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

Diguanylate cyclase PleD (2v0n)

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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 (, ).

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