ArticleStructure (London, England : 1993)2009
Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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106 citing papers in PubMed.
- Atypical β-strand insertion mediates the noncovalent cross-linking in amyloid aggregates.Nature communications · 2026Article
- Secretins of type-two secretion systems are necessary for exopolymeric slime secretion in cyanobacteria and myxobacteria.Nature communications · 2025Article
- Progress toward new function and design of extracellular G protein-coupled receptor nanobodies.Molecular pharmacology · 2025Review
- Cryo-Electron Microscopy of BfpB Reveals a Type IVb Secretin Multimer Adapted to Accommodate the Exceptionally Wide Bundle-Forming Pilus.Pathogens (Basel, Switzerland) · 2025Article
- Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025Article
- Insights into dynamics and gating properties of T2SS secretins.Science advances · 2023Article
- Studying the characteristics of nanobody CDR regions based on sequence analysis in combination with 3D structures.Journal, genetic engineering & biotechnology · 2022Article
- Nanobody-aided crystallization of the transcription regulator PaaR2 from Escherichia coli O157:H7.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Analysis of diverse eukaryotes suggests the existence of an ancestral mitochondrial apparatus derived from the bacterial type II secretion system.Nature communications · 2021Article
- The Leptospiral General Secretory Protein D (GspD), a secretin, elicits complement-independent bactericidal antibody against diverseVaccine: X · 2021Article
- Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell.Metallomics : integrated biometal science · 2020Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Core architecture of a bacterial type II secretion system.Nature communications · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Characterization and structure determination of a llama-derived nanobody targeting the J-base binding protein 1.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Structural insight into the assembly of the type II secretion system pilotin-secretin complex from enterotoxigenic Escherichia coli.Nature microbiology · 2018Article
- Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein.PloS one · 2018Article
- Article
- Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization.PLoS pathogens · 2017Article
46 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
Secretins are among the largest bacterial outer membrane proteins known. Here we report the crystal structure of the periplasmic N-terminal domain of GspD (peri-GspD) from the type 2 secretion system (T2SS) secretin in complex with a nanobody, the VHH domain of a heavy-chain camelid antibody. Two different crystal forms contained the same compact peri-GspD:nanobody heterotetramer. The nanobody contacts peri-GspD mainly via CDR3 and framework residues. The peri-GspD structure reveals three subdomains, with the second and third subdomains exhibiting the KH fold which also occurs in ring-forming proteins of the type 3 secretion system. The first subdomain of GspD is related to domains in phage tail proteins and outer membrane TonB-dependent receptors. A dodecameric peri-GspD model is proposed in which a solvent-accessible beta strand of the first subdomain interacts with secreted proteins and/or T2SS partner proteins by beta strand complementation.
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