Enzyme illuminates bacterial ubiquitination

STRUCTURAL BIOLOGY Structural analysis reveals how a bacterial enzyme catalyses attachment of the protein tag ubiquitin to host proteins, illuminating a process that allows pathogenic bacteria to subvert host-cell function. [...]His407 activates the hydroxyl group of a serine residue on the target p...

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Bibliographic Details
Published in:Nature (London) 2018-05, Vol.557 (7707), p.644-645
Main Authors: Wong, Kathy, Gehring, Kalle
Format: Article
Language:English
Subjects:
Enzymes
Proteins
Structural analysis
Ubiquitination
Online Access:Get full text
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Summary:STRUCTURAL BIOLOGY Structural analysis reveals how a bacterial enzyme catalyses attachment of the protein tag ubiquitin to host proteins, illuminating a process that allows pathogenic bacteria to subvert host-cell function. [...]His407 activates the hydroxyl group of a serine residue on the target protein, which enables the attachment of PR-Ub to the serine. [...]perhaps the most exciting question still to be answered is this: do enzymes that mediate this type of ubiquitination process also exist in eukaryotes?
ISSN:0028-0836
1476-4687
DOI:10.1038/d41586-018-05250-6