ArticleMolecular microbiology2012
Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Recombinant TadZ from the type IVc pilus system induces protective immunity against virulentFrontiers in immunology · 2026Article
- Article
- The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.Nature communications · 2025Article
- Bidirectional pilus processing in the Tad pilus system motor CpaF.Nature communications · 2024Article
- Article
- Article
- Assembly mechanism of a Tad secretion system secretin-pilotin complex.Nature communications · 2023Article
- Septum site placement inMicrobiology (Reading, England) · 2023Article
- Transcriptome analysis revealed growth phase-associated changes of a centenarian-originated probiotic Bifidobacterium animalis subsp. lactis A6.BMC microbiology · 2022Article
- Article
- Diversification of the type IV filament superfamily into machines for adhesion, protein secretion, DNA uptake, and motility.PLoS biology · 2019Article
- Delineation of polar localization domains of Agrobacterium tumefaciens type IV secretion apparatus proteins VirB4 and VirB11.MicrobiologyOpen · 2014Article
- Redefining the PF06864 Pfam family based on Burkholderia pseudomallei PilO2(Bp) S-SAD crystal structure.PloS one · 2014Article
- A multidomain hub anchors the chromosome segregation and chemotactic machinery to the bacterial pole.Genes & development · 2012Article
- The ParA/MinD family puts things in their place.Trends in microbiology · 2012Review
- Mechanism of the asymmetric activation of the MinD ATPase by MinE.Molecular microbiology · 2012Article
- The product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitans.Molecular microbiology · 2012Article
Corrections and comments
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Authors and funding
14 authors at 7 institutions in 1 country.
Funding
Abstract
The tad (tight adherence) locus encodes a protein translocation system that produces a novel variant of type IV pili. The pilus assembly protein TadZ (called CpaE in Caulobacter crescentus) is ubiquitous in tad loci, but is absent in other type IV pilus biogenesis systems. The crystal structure of TadZ from Eubacterium rectale (ErTadZ), in complex with ATP and Mg(2+) , was determined to 2.1 Å resolution. ErTadZ contains an atypical ATPase domain with a variant of a deviant Walker-A motif that retains ATP binding capacity while displaying only low intrinsic ATPase activity. The bound ATP plays an important role in dimerization of ErTadZ. The N-terminal atypical receiver domain resembles the canonical receiver domain of response regulators, but has a degenerate, stripped-down 'active site'. Homology modelling of the N-terminal atypical receiver domain of CpaE indicates that it has a conserved protein-protein binding surface similar to that of the polar localization module of the social mobility protein FrzS, suggesting a similar function. Our structural results also suggest that TadZ localizes to the pole through the atypical receiver domain during an early stage of pili biogenesis, and functions as a hub for recruiting other pili components, thus providing insights into the Tad pilus assembly process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.