Difference between revisions of "Part:BBa K2012002"

Revision as of 07:31, 5 September 2016

PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) 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.

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.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 14
Illegal BamHI site found at 1172
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 430
Illegal NgoMIV site found at 577
Illegal AgeI site found at 913
1000
INCOMPATIBLE WITH RFC[1000]
Illegal BsaI site found at 87

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 https://parts.igem.org/Special:UploadStash/thumb/14afkkce3lm8.ecu58r.14818.png/500px-14afkkce3lm8.ecu58r.14818.png
-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
   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.