Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for effector recognition by an antibacterial type IV secretion system.

Proceedings of the National Academy of Sciences of the United States of America - 4 Jan 2022

Oka Gabriel U, Souza Diorge P, Cenens William, Matsuyama Bruno Y, Cardoso Marcus V C, Oliveira Luciana C, da Silva Lima Filipe, Cuccovia Iolanda M, Guzzo Cristiane R, Salinas Roberto K, Farah Chuck S

Abstract excerpt

Many soil-, water-, and plant-associated bacterial species from the orders Xanthomonadales, Burkholderales, and Neisseriales carry a type IV secretion system (T4SS) specialized in translocating effector proteins into other gram-negative species, leading to target cell death. These effectors, known as X-Tfes, carry a carboxyl-terminal domain of ∼120 residues, termed XVIPCD, characterized by several conserved...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-Bacterial Agents
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Models, Molecular

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Domains

Share to Structure-Activity Relationship

Share to Xanthomonas

Source

Open in PubMed Open full text

Identifiers

PMID: 34983846
DOI: 10.1073/pnas.2112529119
PMCID: PMC8740702

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for effector recognition by an antibacterial type IV secretion system.PMID 34983846Read ↗

Breaching the cell-envelope barriers of gram-positive and fungal microbes by a type VI secretion system in <i>Acidovorax citrulli</i>Semantic proximity Read ↗

Type VI Secretion Effectors: Methodologies and Biology.Semantic proximity Read ↗

Searching Algorithm for Type IV Effector proteins (S4TE) 2.0: improved tools for type IV effector prediction, analysis and comparisonSemantic proximity Read ↗

Functional characterization of the type III secretion ATPase HrcN from the plant pathogen Xanthomonas campestris pv. vesicatoria.Semantic proximity Read ↗

Identification of novel Xanthomonas euvesicatoria type III effector proteins by a machine-learning approach.Semantic proximity Read ↗

The structural landscape and diversity of <i>Pyricularia oryzae</i> MAX effectors revisitedSemantic proximity Read ↗

A Novel Periplasmic Protein, VrpA, Contributes to Efficient Protein Secretion by the Type III Secretion System in Xanthomonas spp.Semantic proximity Read ↗

The inner membrane protein HrcV from Xanthomonas spp. is involved in substrate docking during type III secretion.Semantic proximity Read ↗

Comprehension of Antimicrobial Peptides Modulation of the Type VI Secretion System in <i>Vibrio cholerae</i>Semantic proximity Read ↗

Deciphering the structural intricacy in virulence effectors for proton-motive force mediated unfolding and type-III protein secretionSemantic proximity Read ↗

X-ray crystal structures of the type IVb secretion system DotB ATPases.Semantic proximity Read ↗

Structural insights into substrate recognition by the type VII secretion systemSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.