ArticleJournal of molecular biology2015
Structures of the Ultra-High-Affinity Protein-Protein Complexes of Pyocins S2 and AP41 and Their Cognate Immunity Proteins from Pseudomonas aeruginosa.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
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- Molecular and functional analysis of a putative pyocin S9, with endonuclease activity from P. chlororaphis subsp aurantiaca PB-St2.Archives of microbiology · 2025Article
- Structural basis for the type I-F Cas8-HNH system.The EMBO journal · 2024Article
- Outer membrane translocation of pyocins via the copper regulated TonB-dependent transporter CrtA.The Biochemical journal · 2023Article
- Structural design principles for specific ultra-high affinity interactions between colicins/pyocins and immunity proteins.Scientific reports · 2021Article
- Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.Journal of bacteriology · 2020Article
- Lysocins: Bioengineered Antimicrobials That Deliver Lysins across the Outer Membrane of Gram-Negative Bacteria.Antimicrobial agents and chemotherapy · 2019Article
- A Colicin M-Type Bacteriocin from Pseudomonas aeruginosa Targeting the HxuC Heme Receptor Requires a Novel Immunity Partner.Applied and environmental microbiology · 2018Article
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- Performance of MDockPP in CAPRI rounds 28-29 and 31-35 including the prediction of water-mediated interactions.Proteins · 2017Article
- Performance of ZDOCK and IRAD in CAPRI rounds 28-34.Proteins · 2017Article
- A Natural ChimericmBio · 2017Article
- Novel Immunity Proteins Associated with Colicin M-like Bacteriocins Exhibit Promiscuous Protection inFrontiers in microbiology · 2017Article
- Structural and biophysical analysis of nuclease protein antibiotics.The Biochemical journal · 2016Article
- Determination of Acquired Resistance Profiles ofJundishapur journal of microbiology · 2016Article
- Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.The Biochemical journal · 2016Article
- Draft Genome Sequence of Pseudomonas putida BW11M1, a Banana Rhizosphere Isolate with a Diversified Antimicrobial Armamentarium.Genome announcements · 2016Article
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
How ultra-high-affinity protein-protein interactions retain high specificity is still poorly understood. The interaction between colicin DNase domains and their inhibitory immunity (Im) proteins is an ultra-high-affinity interaction that is essential for the neutralisation of endogenous DNase catalytic activity and for protection against exogenous DNase bacteriocins. The colicin DNase-Im interaction is a model system for the study of high-affinity protein-protein interactions. However, despite the fact that closely related colicin-like bacteriocins are widely produced by Gram-negative bacteria, this interaction has only been studied using colicins from Escherichia coli. In this work, we present the first crystal structures of two pyocin DNase-Im complexes from Pseudomonas aeruginosa, pyocin S2 DNase-ImS2 and pyocin AP41 DNase-ImAP41. These structures represent divergent DNase-Im subfamilies and are important in extending our understanding of protein-protein interactions for this important class of high-affinity protein complex. A key finding of this work is that mutations within the immunity protein binding energy hotspot, helix III, are tolerated by complementary substitutions at the DNase-Immunity protein binding interface. Im helix III is strictly conserved in colicins where an Asp forms polar interactions with the DNase backbone. ImAP41 contains an Asp-to-Gly substitution in helix III and our structures show the role of a co-evolved substitution where Pro in DNase loop 4 occupies the volume vacated and removes the unfulfilled hydrogen bond. We observe the co-evolved mutations in other DNase-Immunity pairs that appear to underpin the split of this family into two distinct groups.
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