Difference between revisions of "Part:BBa K2012002"
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<partinfo>BBa_K2012002 short</partinfo> | <partinfo>BBa_K2012002 short</partinfo> | ||
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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. | 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. | PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) domain. | ||
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Mechanistic Model of PleD Regulation(Wassmann, Chan et al. 2007)<br> | Mechanistic Model of PleD Regulation(Wassmann, Chan et al. 2007)<br> | ||
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 | ||
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Reference:<hr / > | Reference:<hr / > | ||
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. | ||
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− | + | <!-- Add more about the biology of this part here--> | |
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===Usage and Biology=== | ===Usage and Biology=== | ||
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K2012002 SequenceAndFeatures</partinfo> | <partinfo>BBa_K2012002 SequenceAndFeatures</partinfo> | ||
− | <!-- Uncomment this to enable Functional Parameter display | + | <!-- Uncomment this to enable Functional Parameter display --> |
===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K2012002 parameters</partinfo> | <partinfo>BBa_K2012002 parameters</partinfo> | ||
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Revision as of 07:40, 5 September 2016
__NOTOC__
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. ===Usage and Biology=== Sequence and Features