Structural study of the Fox-1 RRM protein hydration reveals a role for key water molecules in RRM-RNA recognition.

ABSTRACT: The Fox-1 RNA recognition motif (RRM) domain is an important member of the RRM protein family. We report a 1.8 Å X-ray structure of the free Fox-1 containing six distinct monomers. We use this and the nuclear magnetic resonance (NMR) structure of the Fox-1 protein/RNA complex for molecular dynamics (MD) analyses of the structured hydration. The individual monomers of the X-ray structure show diverse hydration patterns, however, MD excellently reproduces the most occupied hydration sites. Simulations of the protein/RNA complex show hydration consistent with the isolated protein complemented by hydration sites specific to the protein/RNA interface. MD predicts intricate hydration sites with water-binding times extending up to hundreds of nanoseconds. We characterize two of them using NMR spe

SUBMITTER: Krepl M 

PROVIDER: S-EPMC5737849 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature