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Deciphering the catalytic mechanism of bacterial ubiquitination
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.
Ubiquitination is a type of protein modification in which the protein ubiquitin is attached to a target protein. In eukaryotes (organisms that include fungi, plants and animals), the addition of a ubiquitin tag can act as a signal for various cellular processes. A prime example is the destruction of ubiquitinated proteins by a eukaryotic protein complex called the proteasome. The ubiquitination process is also the target of many bacterial pathogens, which have developed techniques to hijack it for their own benefit. In papers in Nature, Akturk et al.1, Dong et al.2 and Kalayil et al.3 describe the X-ray crystal structure of the bacterial enzyme SdeA, which catalyses ubiquitination. And, writing in Cell, Wang et al.4 report the structure of a bacterial enzyme called SidE from the same protein family as SdeA.