期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 12, 页码 1293-1301出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1511
关键词
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资金
- US National Institutes of Health [GM62414-01]
- Ontario Research and Development Challenge Fund
- Canadian Institutes of Health Research
- Canadian Institutes of Health Research [MT012466, MOP- 57795]
- National Cancer Institute of Canada
- Royal Society and the Scottish Universities Life Sciences Alliance
IpaH proteins are E3 ubiquitin ligases delivered by the type III secretion apparatus into host cells upon infection of humans by the Gram-negative pathogen Shigella flexneri. These proteins comprise a variable leucine-rich repeat-containing N-terminal domain and a conserved C-terminal domain harboring an invariant cysteine residue that is crucial for activity. IpaH homologs are encoded by diverse animal and plant pathogens. Here we demonstrate that the IpaH C-terminal domain carries the catalytic activity for ubiquitin transfer and that the N-terminal domain carries the substrate specificity. The structure of the IpaH C-terminal domain, determined to 2.65-A resolution, represents an all-helical fold bearing no resemblance to previously defined E3 ubiquitin ligases. The conserved and essential cysteine residue lies on a flexible, surface-exposed loop surrounded by conserved acidic residues, two of which are crucial for IpaH activity.
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