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PleD

Contents

Overview

Diguanylate cyclase PleD (1w25)


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)


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. MODEL.
















Allosteric product binding site

Allosteric product binding site


C-di-GMP


Primary inhibition site (Ip)


Secondary inhibition site (Is)


Primary and secondary inhibition sites





Two conformations

non-activated (1w25)
non-activated (1w25)
activated (BeF3- modified; 2v0n)
activated (BeF3- modified; 2v0n)


non-activated (1w25)

activated (BeF3- modified; 2v0n)

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Tilman Schirmer

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