Difference between revisions of "Part:BBa K2012002"
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The DGC domain (green) is connected via a flexible linker to the stem (receiver domain D1 [red] and adaptor domain D2 <br>[yellow]) and is supposed to be mobile relative to it. (Upper row) Activation. Phosphorylation of domain D1 leads to <br>a rearrangement of the stem domains, which, in turn, allows for formation of a tight dimeric stem (3). The dimericarrangement | The DGC domain (green) is connected via a flexible linker to the stem (receiver domain D1 [red] and adaptor domain D2 <br>[yellow]) and is supposed to be mobile relative to it. (Upper row) Activation. Phosphorylation of domain D1 leads to <br>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<br>(4). (Lower row) Product inhibition. Dimeric product molecules, (c-di-GMP)2, can crosslink the primary inhibition site on DGC, Ip,<br> with a secondary binding site either on D2, Is,D2 (5) or on the adjacent DGC domain, Is,DGC(6). The DGC domains become <br>immobilized, and the active sites are hampered from a productive encounter. Note that a possible direct communication between<br> Ip and A sites is not depicted. | is a prerequisite for an efficient and productive encounter of the two substrate-loaded DGC domains to form the c-di-GMP product<br>(4). (Lower row) Product inhibition. Dimeric product molecules, (c-di-GMP)2, can crosslink the primary inhibition site on DGC, Ip,<br> with a secondary binding site either on D2, Is,D2 (5) or on the adjacent DGC domain, Is,DGC(6). The DGC domains become <br>immobilized, and the active sites are hampered from a productive encounter. Note that a possible direct communication between<br> Ip and A sites is not depicted. | ||
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| − | + | Reference:<br / > | |
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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. | 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. | ||
</p> | </p> | ||
Revision as of 07:46, 5 September 2016
__NOTOC__
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:
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.