PDBsum entry 5b0t

Ligase

PDB id: 5b0t

Contents

Protein chain

220 a.a.

Waters ×52

PDB id:

5b0t

Name:

Ligase

Title:

Structure of shigella effector lrr domain

Structure:

E3 ubiquitin-protein ligase ipah9.8. Chain: a. Fragment: unp residues 21-244. Synonym: invasion plasmid antigen ipah9.8. Engineered: yes

Source:

Shigella flexneri. Organism_taxid: 623. Gene: ipah9.8, cp0226, pwr501_0234, sflp090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.214 R-free: 0.265

Authors:

K.Takagi,C.Sasakawa,M.Kim,T.Mizushima

Key ref:

K.Takagi et al. (2016). Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8. Acta Crystallogr F Struct Biol Commun, 72, 269-275. PubMed id: 27050259 DOI: 10.1107/S2053230X16002715

Date:

04-Nov-15 Release date: 06-Apr-16

Protein chain

Q8VSC3  (IPA9_SHIFL) -  E3 ubiquitin-protein ligase ipaH9.8 from Shigella flexneri

Seq: 545 a.a.

Struc: 220 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

DOI no: 10.1107/S2053230X16002715

Acta Crystallogr F Struct Biol Commun 72:269-275 (2016)

PubMed id: 27050259

Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8.

K.Takagi, M.Kim, C.Sasakawa, T.Mizushima.

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.