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Trends Biochem Sci. 2014 Mar;39(3):121-9. doi: 10.1016/j.tibs.2014.01.001. Epub 2014 Feb 5.

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

Author information

1
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, Building E, B-1050 Brussel, Belgium; Department of Structural Biology, VIB, Pleinlaan 2, Building E, B-1050 Brussel, Belgium. Electronic address: agarciap@vub.ac.be.
2
Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Baddiley-Clark Building, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
3
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, Building E, B-1050 Brussel, Belgium; Department of Structural Biology, VIB, Pleinlaan 2, Building E, B-1050 Brussel, Belgium.

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.

PMID:
24507752
DOI:
10.1016/j.tibs.2014.01.001
[Indexed for MEDLINE]

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