5MFU

PA3825-EAL Mn-pGpG Structure

Summary for 5MFU

• Entry DOI: 10.2210/pdb5mfu/pdb
• Related: 4Y8E 4Y9M 4Y9N 4Y9O 4Y9P 4Y9Q 5M1T 5MF5
• Descriptor: cyclic-guanylate-specific phosphodiesterase, RNA (pGpG), MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: eal, phosphodiesterase, biofilm formation, p aeruginosa, pa3825, hydrolase
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 2
• Total formula weight: 28948.63

Authors

Horrell, S.,Bellini, D.,Strange, R.,Wagner, A.,Walsh, M. (deposition date: 2016-11-18, release date: 2017-03-01, Last modification date: 2025-12-17)

Primary citation

Bellini, D.,Horrell, S.,Hutchin, A.,Phippen, C.W.,Strange, R.W.,Cai, Y.,Wagner, A.,Webb, J.S.,Tews, I.,Walsh, M.A.
Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases.
Sci Rep, 7:42166-42166, 2017

PubMed Abstract: The bacterial second messenger cyclic di-3',5'-guanosine monophosphate (c-di-GMP) is a key regulator of bacterial motility and virulence. As high levels of c-di-GMP are associated with the biofilm lifestyle, c-di-GMP hydrolysing phosphodiesterases (PDEs) have been identified as key targets to aid development of novel strategies to treat chronic infection by exploiting biofilm dispersal. We have studied the EAL signature motif-containing phosphodiesterase domains from the Pseudomonas aeruginosa proteins PA3825 (PA3825) and PA1727 (MucR). Different dimerisation interfaces allow us to identify interface independent principles of enzyme regulation. Unlike previously characterised two-metal binding EAL-phosphodiesterases, PA3825 in complex with pGpG provides a model for a third metal site. The third metal is positioned to stabilise the negative charge of the 5'-phosphate, and thus three metals could be required for catalysis in analogy to other nucleases. This newly uncovered variation in metal coordination may provide a further level of bacterial PDE regulation.

PubMed: 28186120
DOI: 10.1038/srep42166

Experimental method

X-RAY DIFFRACTION (2.15 Å)