Binding of cyclic diguanylate in the non-catalytic EAL domain of FimX induces a long-range conformational change.

ABSTRACT: FimX is a multidomain signaling protein required for type IV pilus biogenesis and twitching motility in the opportunistic pathogen Pseudomonas aeruginosa. FimX is localized to the single pole of the bacterial cell, and the unipolar localization is crucial for the correct assembly of type IV pili. FimX contains a non-catalytic EAL domain that lacks cyclic diguanylate (c-di-GMP) phosphodiesterase activity. It was shown that deletion of the EAL domain or mutation of the signature EVL motif affects the unipolar localization of FimX. However, it was not understood how the C-terminal EAL domain could influence protein localization considering that the localization sequence resides in the remote N-terminal region of the protein. Using hydrogen/deuterium exchange-coupled mass spectrometry, we foun

SUBMITTER: Qi Y 

PROVIDER: S-EPMC3024786 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature