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Diguanylate cyclase

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(New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> == Function == '''Diguanylate cyclase''' (DGC) catalyzes the conversion of GTP to c...)
Current revision (09:57, 21 December 2022) (edit) (undo)
 
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<StructureSection load='' size='350' side='right' caption='Diguanylate cyclase GGDEF domain complex with cyclic di-GMP, Mg+2 ion (green) and PEG (PDB code [[3qyy]]).' scene='67/677040/Cv/1'>
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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== Function ==
== Function ==
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'''Diguanylate cyclase''' (DGC) catalyzes the conversion of GTP to cyclic di-GMP and diphosphate. DGC contains the sequence motif GGDEF in its active site. For more details see [[PleD catalysis]].
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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 />
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[[PleD catalysis]]<br />
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== Disease ==
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[[PleD activation]]<br />
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[[PleD allosteric product inhibition]]<br />
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[[C-di-GMP signaling]].
== Relevance ==
== Relevance ==
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DGC from ''Borrelia burgdorferi'' is involved in the transmission of spirochetes from ticks to mammals causing Lyme Disease.
== Structural highlights ==
== Structural highlights ==
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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]], [[4urs]] – 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 />
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**[3ign]] – DGC GGDEF domain – ''Marinobacter aquaeolei''<br />
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**[[3ign]] – MaDGC GGDEF domain – ''Marinobacter aquaeolei''<br />
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**[[4kg1]] – DGC residues 1-150 – ''Xanthomonas campestris''<br />
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**[[3h9w]] – MaDGC N terminal<br />
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**[[4zmu]] – PaDGC – ''Pseudomonas aeruginosa''<br />
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**[[3hvw]], [[4iob]] – DGC GGDEF domain 254-414<br />
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**[[7a7e]] – PaDGC GGDEF domain (mutant)<br />
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**[[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 />
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**[[3n53]] – DGC – ''Pelobacter carbinolicus''<br />
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**[[5h5o]] – XcDGC residues 1-150 – ''Xanthomonas campestris''<br />
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**[[3qyy]] – XcDGC GGDEF domain + cyclic di-GMP <br />
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**[[4urs]] – TmDGC GGDEF domain + cyclic di-GMP<br />
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**[[3t9o]] – EcDGC YDEH CZB domain – ''Escherichia coli''<br />
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**[[3tvk]], [[4zve]], [[4zvg]], [[4zvh]] – EcDGC YDEH GGDEF domain <br />
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**[[4h54]] – EcDGC YDEH (mutant) <br />
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**[[4zva]], [[4zvb]] – EcDGC globin domain <br />
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**[[4zvc]], [[4zvd]] – EcDGC mid domain <br />
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**[[4zvf]] – EcDGC GGDEF domain 297-460 + GTP derivative<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 />
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**[[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 />
*Response regulator PleD
*Response regulator PleD
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**[[1w25]], [[2wb4]] – CvDGC + C-diGMP – ''Caulobacter vibrioides''<br />
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**[[1w25]], [[2wb4]] – CvDGC + cyclic di-GMP <br />
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**[[2v0n]] – CvDGC + C-diGMP + GTP<br />
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**[[2v0n]] – CvDGC + cyclic di-GMP + GTP<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
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[[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 21-December-2022

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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