The many faces of Fic: structural and functional aspects of Fic enzymes

Abel Garcia Pino, Nikolay Zenkin, Remy Loris

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)

Abstract

Fic enzymes post-translationally modify proteins through AMPylation, UMPylation, phosphorylation, or
phosphocholination. They have been identified across all domains of life, and they target a myriad of proteins such as eukaryotic GTPases, unstructured protein segments, and bacterial enzymes. Consequently, they play crucial roles in eukaryotic signal transduction, drug tolerance, bacterial pathogenicity, and the bacterial stress response. Structurally, they consist of an all a-helical core domain that supports and scaffolds a structurally conserved active-site loop, which catalyses the transfer of various parts of a nucleotide cofactor to proteins. Despite their diverse substrates and targets, they retain a conserved active site and reaction chemistry. This catalytic variety came to light only recently with the crystal structures of different Fic enzymes.
Original languageEnglish
Pages (from-to)121-129
Number of pages9
JournalTrends in Biochemical Sciences
Volume39
Publication statusPublished - 5 Feb 2014

Keywords

  • Persistence
  • Bacterial pathogenicity
  • Structural biology
  • Toxin-Antitoxin module

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