ArticleScientific reports2017
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- Increased Expression of Bacterial Cellulose Synthase Genes inBiomacromolecules · 2025Article
- Modulating Microbial Materials - Engineering Bacterial Cellulose with Synthetic Biology.ACS synthetic biology · 2024Review
- Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope.Nature communications · 2024Article
- Molecular insights into phosphoethanolamine cellulose formation and secretion.bioRxiv : the preprint server for biology · 2024Article
- The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing.PLoS pathogens · 2022Article
- Weaving of bacterial cellulose by the Bcs secretion systems.FEMS microbiology reviews · 2022Review
- Structural snapshot of a glycoside hydrolase family 8 endo-β-1,4-glucanase capturing the state after cleavage of the scissile bond.Acta crystallographica. Section D, Structural biology · 2022Article
- Comparative Genome Analysis of ThreeFrontiers in microbiology · 2021Article
- Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa.Structure (London, England : 1993) · 2020Article
- A novel FLOURY ENDOSPERM2 (FLO2)-interacting protein, is involved in maintaining fertility and seed quality in rice.Plant biotechnology (Tokyo, Japan) · 2020Article
- Architecture of the Cellulose Synthase Outer Membrane Channel and Its Association with the Periplasmic TPR Domain.Structure (London, England : 1993) · 2019Article
- Effect of ethanol supplementation on the transcriptional landscape of bionanocellulose producer Komagataeibacter xylinus E25.Applied microbiology and biotechnology · 2019Article
- Structural features underlying recognition and translocation of extracellular polysaccharides.Interface focus · 2019Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains.
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