User:Tilman Schirmer/Sandbox 211

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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

(
Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.
)===

After binding of the it is believed that two GGDEF domains associate antiparallely to form a catalytically competent dimer (, ).

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Tilman Schirmer

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