Revision as of 07:37, 5 September 2016

__NOTOC__<\h1> BBa_K2012002 short Intracellular c-di-GMP concentration has been regulated by two functionally opposing enzymes, the diguanylate cyclases (DGCs) containing a GGDEF domain, and phosphodiesterases (PDEs) containing either an EAL or HD-GYP domain. PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) domain. Mechanistic Model of PleD Regulation(Wassmann, Chan et al. 2007)
The DGC domain (green) is connected via a flexible linker to the stem (receiver domain D1 [red] and adaptor domain D2
[yellow]) and is supposed to be mobile relative to it. (Upper row) Activation. Phosphorylation of domain D1 leads to
a rearrangement of the stem domains, which, in turn, allows for formation of a tight dimeric stem (3). The dimericarrangement is a prerequisite for an efficient and productive encounter of the two substrate-loaded DGC domains to form the c-di-GMP product
(4). (Lower row) Product inhibition. Dimeric product molecules, (c-di-GMP)2, can crosslink the primary inhibition site on DGC, Ip,
with a secondary binding site either on D2, Is,D2 (5) or on the adjacent DGC domain, Is,DGC(6). The DGC domains become
immobilized, and the active sites are hampered from a productive encounter. Note that a possible direct communication between
Ip and A sites is not depicted. Reference:

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Wassmann, P., et al. (2007). "Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition." Structure 15(8): 915-927. Sequence and Features BBa_K2012002 SequenceAndFeatures <\html>