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Crystal structure of the substrate‐recognition domain of the Shigella E3 ligase IpaH9.8
Author(s) -
Takagi Kenji,
Kim Minsoo,
Sasakawa Chihiro,
Mizushima Tsunehiro
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16002715
Subject(s) - ubiquitin ligase , effector , virulence , shigella , dna ligase , ubiquitin , biology , bacteria , leucine rich repeat , shigella flexneri , microbiology and biotechnology , escherichia coli , genetics , gene , kinase , salmonella
Infectious diseases caused by bacteria have significant impacts on global public health. During infection, pathogenic bacteria deliver a variety of virulence factors, called effectors, into host cells. The Shigella effector IpaH9.8 functions as an ubiquitin ligase, ubiquitinating the NF‐κB essential modulator (NEMO)/IKK‐γ to inhibit host inflammatory responses. IpaH9.8 contains leucine‐rich repeats (LRRs) involved in substrate recognition and an E3 ligase domain. To elucidate the structural basis of the function of IpaH9.8, the crystal structure of the LRR domain of Shigella IpaH9.8 was determined and this structure was compared with the known structures of other IpaH family members. This model provides insights into the structural features involved in substrate specificity.