Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases.

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^EAL) and PA1727 (MucR^EAL). Different dimerisation interfaces allow us to identify interface independent principles of enzyme regulation. Unlike previously characterised two-metal binding EAL-phosphodiesterases, PA3825^EAL in complex with pGpG pro

SUBMITTER: Bellini D 

PROVIDER: S-EPMC5301497 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature