Diguanylate cyclase

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'''Diguanylate cyclase''' (DGC) catalyzes the conversion of GTP to [[C-di-GMP]] and diphosphate. <ref>PMID:17697992</ref> For more details see<br />
'''Diguanylate cyclase''' (DGC) catalyzes the conversion of GTP to [[C-di-GMP]] and diphosphate. <ref>PMID:17697992</ref> For more details see<br />
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[[PleD catalysis]]<br />
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[[PleD activation]]<br />
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[[PleD allosteric product inhibition]]<br />
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[[C-di-GMP signaling]].
[[C-di-GMP signaling]].
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== Structural highlights ==
== Structural highlights ==
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DGC contains the sequence <scene name='67/677040/Cv/2'>motif GGDEF</scene> in its active site. <scene name='67/677040/Cv/3'>Cyclic di-GMP and Mg+2 ions interact with two monomers</scene> of DGC.<ref>PMID:22120736</ref>
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DGC contains the sequence <scene name='67/677040/Cv/4'>motif GGDEF</scene> in its active site. <scene name='67/677040/Cv/5'>Cyclic di-GMP and Mg+2 ions interact with two monomers</scene> of DGC.<ref>PMID:22120736</ref>
</StructureSection>
</StructureSection>
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*DGC
*DGC
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**[[4urg]] – TmDGC GGDEF domain – ''Thermotoga maritima''<br />
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**[[4urg]], [[6khu]] – TmDGC GGDEF domain 82-248 – ''Thermotoga maritima''<br />
**[[4urq]] – TmDGC GGDEF domain (mutant)<br />
**[[4urq]] – TmDGC GGDEF domain (mutant)<br />
**[[3ign]] – MaDGC GGDEF domain – ''Marinobacter aquaeolei''<br />
**[[3ign]] – MaDGC GGDEF domain – ''Marinobacter aquaeolei''<br />
**[[3h9w]] – MaDGC N terminal<br />
**[[3h9w]] – MaDGC N terminal<br />
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**[[4zmu]] – PaDGC – ''Pseudomonas aeruginosa''<br />
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**[[8wcn]] – PaDGC + GMPCPP – ''Pseudomonas aeruginosa'' – Cryo EM<br />
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**[[3hvw]], [[4iob]] – DGC GGDEF domain <br />
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**[[4zmu]] – PaDGC 1-341 <br />
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**[[3hvw]], [[4iob]] – DGC GGDEF domain 254-414<br />
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**[[7a7e]] – PaDGC GGDEF domain (mutant)<br />
**[[4zmm]] – PaDGC GGDEF domain + C-diGMP<br />
**[[4zmm]] – PaDGC GGDEF domain + C-diGMP<br />
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**[[5m3c]] – PaDGC GGDEF domain + GTP<br />
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**[[7e6g]] – PaDGC GGDEF domain + SiaC<br />
**[[3n53]] – DGC – ''Pelobacter carbinolicus''<br />
**[[3n53]] – DGC – ''Pelobacter carbinolicus''<br />
**[[5h5o]] – XcDGC residues 1-150 – ''Xanthomonas campestris''<br />
**[[5h5o]] – XcDGC residues 1-150 – ''Xanthomonas campestris''<br />
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**[[4zva]], [[4zvb]] – EcDGC globin domain <br />
**[[4zva]], [[4zvb]] – EcDGC globin domain <br />
**[[4zvc]], [[4zvd]] – EcDGC mid domain <br />
**[[4zvc]], [[4zvd]] – EcDGC mid domain <br />
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**[[4zvf]] – EcDGC GGDEF domain + GTP derivative<br />
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**[[4zvf]] – EcDGC GGDEF domain 297-460 + GTP derivative<br />
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**[[5llw]], [[5lly]] – IdDGC + phytochromobilin - Idiomarina<br />
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**[[6eib]] – DGC GGDEF domain – ''Vibrio cholerae''<br />
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**[[6et7]] – IdDGC (mutant) - ''Idiomarina''<br />
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**[[5llw]], [[5lly]] – IdDGC + phytochromobilin <br />
**[[5llx]] – IdDGC + phytochromobilin + GTP <br />
**[[5llx]] – IdDGC + phytochromobilin + GTP <br />
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**[[6saw]], [[6sax]] – IdDGC chromophore-binding domain 3-312<br />
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**[[6hbz]] – DGCB – ''Bdellovibrio bacteriovorus''<br />
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**[[6tts]] – CvDGCB GGDEF domain 176-353 + C-diGMP – ''Caulobacter vibrioides'' <br />
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**[[6ttr]] – CvDGCB GGDEF+coiled-coil domains 153-353 (mutant) + C-diGMP <br />
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**[[7k5n]] – DGC LBD domain 39-286 + Pro – ''Aeromonas caviae''<br />
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**[[8px4]] – DGC – ''Leptospira interogans''<br />
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**[[8c05]] – DGC + FMN – ''Methylotenera''<br />
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*Response regulator PleD
 
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**[[1w25]], [[2wb4]] – CvDGC + cyclic di-GMP – ''Caulobacter vibrioides''<br />
 
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**[[2v0n]] – CvDGC + cyclic di-GMP + GTP<br />
 
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Diguanylate cyclase GGDEF domain complex with cyclic di-GMP, Mg+2 ion (green) and PEG (PDB code 3qyy).

Drag the structure with the mouse to rotate

3D Structures of diguanylate cyclase

Updated on 02-April-2025

References

  1. ↑ Stock AM. Diguanylate cyclase activation: it takes two. Structure. 2007 Aug;15(8):887-8. PMID:17697992 doi:http://dx.doi.org/10.1016/j.str.2007.07.003
  2. ↑ Yang CY, Chin KH, Chuah ML, Liang ZX, Wang AH, Chou SH. The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)(2) at the active site. Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):997-1008. Epub 2011 Nov, 18. PMID:22120736 doi:10.1107/S090744491104039X

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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