Autor: |
Federico Mantoni, Chiara Scribani Rossi, Alessandro Paiardini, Adele Di Matteo, Loredana Cappellacci, Riccardo Petrelli, Massimo Ricciutelli, Alessio Paone, Francesca Cutruzzolà, Giorgio Giardina, Serena Rinaldo |
Jazyk: |
angličtina |
Rok vydání: |
2021 |
Předmět: |
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Zdroj: |
Life, Vol 11, Iss 1, p 31 (2021) |
Druh dokumentu: |
article |
ISSN: |
2075-1729 |
DOI: |
10.3390/life11010031 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
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