7A7E

Structure of a delta-N mutant - E232start - of PA1120 (TpbB or YfiN) from Pseudomonas aeruginosa (PAO1) comprising only the GGDEF domain

Summary for 7A7E

• Entry DOI: 10.2210/pdb7a7e/pdb
• Descriptor: Diguanylate cyclase TpbB, MAGNESIUM ION (3 entities in total)
• Functional Keywords: c-di-gmp, gtp, diguanylate cyclase, biofilm, ligase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 3
• Total formula weight: 67750.87

Authors

Giardina, G.,Rinaldo, S.,Mantoni, F.,Brunotti, P. (deposition date: 2020-08-28, release date: 2021-07-07, Last modification date: 2024-01-31)

Primary citation

Mantoni, F.,Scribani Rossi, C.,Paiardini, A.,Di Matteo, A.,Cappellacci, L.,Petrelli, R.,Ricciutelli, M.,Paone, A.,Cutruzzola, F.,Giardina, G.,Rinaldo, S.
Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts.
Life, 11:-, 2021

PubMed 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.

PubMed: 33418960
DOI: 10.3390/life11010031

Experimental method

X-RAY DIFFRACTION (2.8 Å)