5B0T

Structure of Shigella effector LRR domain

Summary for 5B0T

• Entry DOI: 10.2210/pdb5b0t/pdb
• Related: 5B0N
• Descriptor: E3 ubiquitin-protein ligase ipaH9.8 (2 entities in total)
• Functional Keywords: effector, ubiquitin ligase, lrr domain, ligase
• Biological source: Shigella flexneri
• Total number of polymer chains: 1
• Total formula weight: 25377.51

Authors

Takagi, K.,Sasakawa, C.,Kim, M.,Mizushima, T. (deposition date: 2015-11-04, release date: 2016-04-06, Last modification date: 2024-03-20)

Primary citation

Takagi, K.,Kim, M.,Sasakawa, C.,Mizushima, T.
Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8
Acta Crystallogr.,Sect.F, 72:269-275, 2016

PubMed Abstract: 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.

PubMed: 27050259
DOI: 10.1107/S2053230X16002715

Experimental method

X-RAY DIFFRACTION (2 Å)