ArticlePLoS pathogens2013
Complex structure of OspI and Ubc13: the molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognition.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Molecular mechanisms of co-infections.EMBO reports · 2025Review
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Acetylation, Phosphorylation, Ubiquitination (Oh My!): Following Post-Translational Modifications on the Ubiquitin Road.Biomolecules · 2022Review
- The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis.The Journal of biological chemistry · 2021Review
- Conformational Insights into the Control of CNF1 Toxin Activity by Peptidyl-Prolyl Isomerization: A Molecular Dynamics Perspective.International journal of molecular sciences · 2021Article
- Legionella effector MavC targets the Ube2N~Ub conjugate for noncanonical ubiquitination.Nature communications · 2020Article
- A bacterial effector deubiquitinase specifically hydrolyses linear ubiquitin chains to inhibit host inflammatory signalling.Nature microbiology · 2019Article
- Cooperative Immune Suppression by Escherichia coli and Shigella Effector Proteins.Infection and immunity · 2018Review
- Exploitation of the host cell ubiquitin machinery by microbial effector proteins.Journal of cell science · 2017Review
- Ubc13: the Lys63 ubiquitin chain building machine.Oncotarget · 2016Review
- HTLV-1 Tax Functions as a Ubiquitin E3 Ligase for Direct IKK Activation via Synthesis of Mixed-Linkage Polyubiquitin Chains.PLoS pathogens · 2016Article
- E2 enzymes: more than just middle men.Cell research · 2016Review
- Alterations of host cell ubiquitination machinery by pathogenic bacteria.Frontiers in cellular and infection microbiology · 2015Review
- Review
- Exploitation of the host ubiquitin system by human bacterial pathogens.Nature reviews. Microbiology · 2014Review
- What a difference a Dalton makes: bacterial virulence factors modulate eukaryotic host cell signaling systems via deamidation.Microbiology and molecular biology reviews : MMBR · 2013Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubc13 is an important ubiquitin-conjugating (E2) enzyme in the NF-κB signaling pathway. The Shigella effector OspI targets Ubc13 and deamidates Gln100 of Ubc13 to a glutamic acid residue, leading to the inhibition of host inflammatory responses. Here we report the crystal structure of the OspI-Ubc13 complex at 2.3 Å resolution. The structure reveals that OspI uses two differently charged regions to extensively interact with the α1 helix, L1 loop and L2 loop of Ubc13. The Gln100 residue is bound within the hydrophilic catalytic pocket of OspI. A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI. The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition. Biochemical results indicate that both of the differently charged regions in OspI are important for the interaction with Ubc13, and the specificity determinants in Ubc13 for OspI recognition reside in the distinct residues in the α1 helix and L2 region. Our study reveals the molecular basis of Ubc13 deamidation by OspI, as well as a convergence of E2 recognition by bacterial and host proteins.
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