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

TitleThe many faces of Fic: structural and functional aspects of Fic enzymes.
Publication TypeJournal Article
Year of Publication2014
AuthorsGarcia-Pino, A., N. Zenkin, and R. Loris
JournalTrends Biochem Sci
Volume39
Issue3
Pagination121-9
Date Published2014 Mar
ISSN0968-0004
KeywordsAnimals, Bacteria, Bacterial Proteins, Crystallography, X-Ray, GTP Phosphohydrolases, Humans, Protein Modification, Translational, Protein Structure, Secondary, Protein Structure, Tertiary, Transferases
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 α-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.

DOI10.1016/j.tibs.2014.01.001
Alternate JournalTrends Biochem. Sci.
PubMed ID24507752
Grant ListBB/J006378/1 / / Biotechnology and Biological Sciences Research Council / United Kingdom
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