Thinking outside the Osp(G) - Kinase activation by E2-ubiquitin

Maarten F. De Jong, Neal M. Alto

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

OspG is a secreted effector kinase from the human pathogen Shigella that is required for the reduction of immune responses during Shigella infection. A new study in The EMBO Journal provides a co-crystal structure of OspG bound to UbcH5c∼Ub, revealing how a bacterial kinase can be activated by the host ubiquitin conjugation machinery. These results provide molecular insight into an enigmatic microbial virulence factor that thwarts the host immune surveillance system to cause disease.

Original languageEnglish (US)
Pages (from-to)403-404
Number of pages2
JournalEMBO Journal
Volume33
Issue number5
DOIs
StatePublished - Mar 3 2014

Fingerprint

Cyclic GMP-Dependent Protein Kinases
Shigella
Ubiquitin
Phosphotransferases
Chemical activation
Virulence Factors
Pathogens
Machinery
Immune System
Crystal structure
Infection

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)

Cite this

Thinking outside the Osp(G) - Kinase activation by E2-ubiquitin. / De Jong, Maarten F.; Alto, Neal M.

In: EMBO Journal, Vol. 33, No. 5, 03.03.2014, p. 403-404.

Research output: Contribution to journalArticle

De Jong, Maarten F. ; Alto, Neal M. / Thinking outside the Osp(G) - Kinase activation by E2-ubiquitin. In: EMBO Journal. 2014 ; Vol. 33, No. 5. pp. 403-404.
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