Diguanylate cyclase
From Proteopedia
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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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[[C-di-GMP signaling]]. | [[C-di-GMP signaling]]. | ||
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**[[3ign]] – MaDGC GGDEF domain – ''Marinobacter aquaeolei''<br /> | **[[3ign]] – MaDGC GGDEF domain – ''Marinobacter aquaeolei''<br /> | ||
**[[3h9w]] – MaDGC N terminal<br /> | **[[3h9w]] – MaDGC N terminal<br /> | ||
| - | **[[ | + | **[[8wcn]] – PaDGC + GMPCPP – ''Pseudomonas aeruginosa'' – Cryo EM<br /> |
| + | **[[4zmu]] – PaDGC 1-341 <br /> | ||
**[[3hvw]], [[4iob]] – DGC GGDEF domain 254-414<br /> | **[[3hvw]], [[4iob]] – DGC GGDEF domain 254-414<br /> | ||
**[[7a7e]] – PaDGC GGDEF domain (mutant)<br /> | **[[7a7e]] – PaDGC GGDEF domain (mutant)<br /> | ||
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**[[6ttr]] – CvDGCB GGDEF+coiled-coil domains 153-353 (mutant) + C-diGMP <br /> | **[[6ttr]] – CvDGCB GGDEF+coiled-coil domains 153-353 (mutant) + C-diGMP <br /> | ||
**[[7k5n]] – DGC LBD domain 39-286 + Pro – ''Aeromonas caviae''<br /> | **[[7k5n]] – DGC LBD domain 39-286 + Pro – ''Aeromonas caviae''<br /> | ||
| + | **[[8px4]] – DGC – ''Leptospira interogans''<br /> | ||
| + | **[[8c05]] – DGC + FMN – ''Methylotenera''<br /> | ||
| - | *Response regulator PleD | ||
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| - | **[[1w25]], [[2wb4]] – CvDGC + cyclic di-GMP <br /> | ||
| - | **[[2v0n]] – CvDGC + cyclic di-GMP + GTP<br /> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of diguanylate cyclase
Updated on 02-April-2025
References
- ↑ 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
- ↑ 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
