Structural highlights
Function
Q9I4L5_PSEAE
Publication Abstract from PubMed
GGDEF-containing proteins respond to different environmental cues to finely modulate cyclic diguanylate (c-di-GMP) levels in time and space, making the allosteric control a distinctive trait of the corresponding proteins. The diguanylate cyclase mechanism is emblematic of this control: two GGDEF domains, each binding one GTP molecule, must dimerize to enter catalysis and yield c-di-GMP. The need for dimerization makes the GGDEF domain an ideal conformational switch in multidomain proteins. A re-evaluation of the kinetic profile of previously characterized GGDEF domains indicated that they are also able to convert GTP to GMP: this unexpected reactivity occurs when conformational issues hamper the cyclase activity. These results create new questions regarding the characterization and engineering of these proteins for in solution or structural studies.
Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts.,Mantoni F, Scribani Rossi C, Paiardini A, Di Matteo A, Cappellacci L, Petrelli R, Ricciutelli M, Paone A, Cutruzzola F, Giardina G, Rinaldo S Life (Basel). 2021 Jan 6;11(1). pii: life11010031. doi: 10.3390/life11010031. PMID:33418960[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mantoni F, Scribani Rossi C, Paiardini A, Di Matteo A, Cappellacci L, Petrelli R, Ricciutelli M, Paone A, Cutruzzolà F, Giardina G, Rinaldo S. Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts. Life (Basel). 2021 Jan 6;11(1):31. PMID:33418960 doi:10.3390/life11010031
