ArticleFEBS open bio2020
Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Mini-bacterioferritins: structural insight into a ferritin-like protein from the anaerobic methane-oxidising archaeon Candidatus Methanoperedens carboxydivorans.Communications biology · 2026Article
- A noncanonical transcriptional regulation in natural product biosynthesis.Nucleic acids research · 2026Article
- Structural Insights into Iron Ions Accumulation in Dps Nanocage.International journal of molecular sciences · 2022Article
- Non-conventional octameric structure of C-phycocyanin.Communications biology · 2021Article
- Structural Rearrangement of Dps-DNA Complex Caused by Divalent Mg and Fe Cations.International journal of molecular sciences · 2021Article
- Enzymatic Antioxidant Signatures in Hyperthermophilic Archaea.Antioxidants (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DNA-binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X-ray crystallographic analysis revealed that TlDps1 possessed His-type ferroxidase centers within the cavity and unique metal-binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability.
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Registered trials
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