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2 results on '"Federico Mantoni"'

1. Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts

Author

Federico Mantoni, Chiara Scribani Rossi, Alessandro Paiardini, Adele Di Matteo, Loredana Cappellacci, Riccardo Petrelli, Massimo Ricciutelli, Alessio Paone, Francesca Cutruzzolà, Giorgio Giardina, and Serena Rinaldo

Subjects
enzyimatic assay, GGDEF, c-di-GMP, allostery, protein engineering, Science
Abstract

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.

Published
2021
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2. Studying ggdef domain in the act: Minimize conformational frustration to prevent artefacts

Author

Serena Rinaldo, Loredana Cappellacci, Francesca Cutruzzolà, Adele Di Matteo, Federico Mantoni, Alessio Paone, Chiara Scribani Rossi, Massimo Ricciutelli, Riccardo Petrelli, Giorgio Giardina, and Alessandro Paiardini

Subjects
0301 basic medicine, GTP', media_common.quotation_subject, 030106 microbiology, Allosteric regulation, Frustration, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, allostery, C-di-GMP, enzyimatic assay, GGDEF, protein engineering, lcsh:Science, Ecology, Evolution, Behavior and Systematics, media_common, biology, Chemistry, Paleontology, Protein engineering, c-di-GMP, GGDEF domain, 030104 developmental biology, Space and Planetary Science, Biophysics, biology.protein, Diguanylate cyclase, lcsh:Q, Cyclase activity
Abstract

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.

Published
2021

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