Versatile roles of protein flavinylation in bacterial extracyotosolic electron transfer.

ABSTRACT: Bacteria perform diverse redox chemistries in the periplasm, cell wall, and extracellular space. Electron transfer for these extracytosolic activities is frequently mediated by proteins with covalently bound flavins, which are attached through post-translational flavinylation by the enzyme ApbE. Despite the significance of protein flavinylation to bacterial physiology, the basis and function of this modification remains unresolved. Here we apply genomic context analyses, computational structural biology, and biochemical studies to address the role of ApbE flavinylation throughout bacterial life. We find that ApbE flavinylation sites exhibit substantial structural heterogeneity. We identify two novel classes of flavinylation substrates that are related to characterized proteins with non-cov

SUBMITTER: Huang S 

PROVIDER: S-EPMC10979944 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature