User:Tilman Schirmer/Sandbox 200
From Proteopedia
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== [[User:Tilman Schirmer/Sandbox 202|C-di-GMP specific phosphodiesterases]] == | == [[User:Tilman Schirmer/Sandbox 202|C-di-GMP specific phosphodiesterases]] == | ||
| - | + | Cleavage of one of the phosphodiester bonds is catalyzed by EAL and HD-GYP domains. Thus, the cylic dinucleotide c-di-GMP is converted to the linear form pGpG. <br><br>Two structures of EAL domain proteins have been determined in complex with substrate c-di-GMP (YkuI and Blrp1) and are presented [[User:Tilman Schirmer/Sandbox 202|here]]. | |
== [[User:Tilman Schirmer/Sandbox 203|C-di-GMP receptors]] == | == [[User:Tilman Schirmer/Sandbox 203|C-di-GMP receptors]] == | ||
Revision as of 20:44, 30 June 2009
Cyclic di-GMP signaling
Contents |
Intro
Diguanylate cyclases
The condensation reaction 2 GTP -> c-di-GMP + 2 PPi is catalyzed by GGDEF domains that typically occur in combination with sensory or regulator domains. The structures of two diguanylate cyclases (PleD and WspR) have been determined, both being response regulators with a response regulator receiver (Rec) and a GGDEF output (effector) domain. Response regulators are activated through phosphorylation of a conserved aspartate by cognate histidine kinases.
PleD
PleD catalysis
PleD activation
PleD allosteric product inhibition
WspR
C-di-GMP specific phosphodiesterases
Cleavage of one of the phosphodiester bonds is catalyzed by EAL and HD-GYP domains. Thus, the cylic dinucleotide c-di-GMP is converted to the linear form pGpG.
Two structures of EAL domain proteins have been determined in complex with substrate c-di-GMP (YkuI and Blrp1) and are presented here.
