ArticleProtein science : a publication of the Protein Society2020
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Beyond movement: the dynamic roles of Type IV pili in cyanobacterial life.Journal of bacteriology · 2025Review
- Profiling the interplay and coevolution ofMicrobiology spectrum · 2024Article
- Crowded environments tune the fold-switching in metamorphic proteins.Communications chemistry · 2023Article
- Comparative Genomics of Synechococcus elongatus Explains the Phenotypic Diversity of the Strains.mBio · 2022Article
- Transcriptomic and Phenomic Investigations Reveal Elements in Biofilm Repression and Formation in the CyanobacteriumFrontiers in microbiology · 2022Article
- Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2.Proteins · 2021Article
- Article
- Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and involved in regulation of biofilm formation in the cyanobacterium Synechococcus elongatus PCC 7942. Se0862 is a class α+β protein with ααββββαα topology and roll architecture, consisting of a four-stranded β-sheet that is flanked by four α-helices on one side. Conserved surface residues constitute a hydrophobic pocket and charged regions that are likely also present in Se0862 orthologs.
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Registered trials
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