4r8z

Structural highlights

Function

CDPD2_PSEAE Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP (PubMed:19170727, PubMed:24066157). Hydrolyzes c-di-GMP to GMP in a two-step reaction, via the linear intermediate 5'-phosphoguanylyl(3'->5')guanosine (pGpG). In vitro, can use pGpG as an alternative substrate and hydrolyze it into GMP (PubMed:24066157). Acts in regulation of motility, synthesis of virulence determinants and biofilm architecture (PubMed:19170727). May act preferentially as a pGpG binding protein (PubMed:24066157).^{[1] [2]}

See Also

• Phosphodiesterase 3D structures

References

1. ↑ Ryan RP, Lucey J, O'Donovan K, McCarthy Y, Yang L, Tolker-Nielsen T, Dow JM. HD-GYP domain proteins regulate biofilm formation and virulence in Pseudomonas aeruginosa. Environ Microbiol. 2009 May;11(5):1126-36. PMID:19170727 doi:10.1111/j.1462-2920.2008.01842.x
2. ↑ Stelitano V, Giardina G, Paiardini A, Castiglione N, Cutruzzolà F, Rinaldo S. C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG. PLoS One. 2013 Sep 16;8(9):e74920. PMID:24066157 doi:10.1371/journal.pone.0074920