ArticleThe Journal of biological chemistry2011
Structure and mechanism of iron translocation by a Dps protein from Microbacterium arborescens.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Self-Assembled Ferritin Nanoparticles for Delivery of Antigens and Development of Vaccines: From Structure and Property to Applications.Molecules (Basel, Switzerland) · 2024Review
- Shape-Anisotropic Assembly of Protein Nanocages with Identical Building Blocks by Designed Intermolecular π-π Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Influence of Cupric (CuInternational journal of molecular sciences · 2023Article
- Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein.Journal of bacteriology · 2022Review
- Structural Insights into Iron Ions Accumulation in Dps Nanocage.International journal of molecular sciences · 2022Article
- Time-Resolved Studies of Ytterbium Distribution at Interfacial Surfaces of Ferritin-like Dps Protein Demonstrate Metal Uptake and Storage Pathways.Biomedicines · 2021Article
- Dps-DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration.European biophysics journal : EBJ · 2021Article
- Comparative Proteomic Analysis ofTurkish journal of pharmaceutical sciences · 2021Article
- An Overview of Dps: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties.Sub-cellular biochemistry · 2021Review
- Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins.The Journal of biological chemistry · 2020Article
- Enzymatic Antioxidant Signatures in Hyperthermophilic Archaea.Antioxidants (Basel, Switzerland) · 2020Review
- Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.FEBS open bio · 2020Article
- Polymorphic Protective Dps-DNA Co-Crystals by Cryo Electron Tomography and Small Angle X-Ray Scattering.Biomolecules · 2019Article
- Large protein organelles form a new iron sequestration system with high storage capacity.eLife · 2019Article
- The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions.Molecules (Basel, Switzerland) · 2017Article
- Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Article
- Ferritin family proteins and their use in bionanotechnology.New biotechnology · 2015Review
- Isolation of cellulolytic bacteria from the intestine of Diatraea saccharalis larvae and evaluation of their capacity to degrade sugarcane biomass.AMB Express · 2015Article
- In vivo Pyro-SIP assessing active gut microbiota of the cotton leafworm, Spodoptera littoralis.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dps (DNA protection during starvation) enzymes are a major class of dodecameric proteins that bacteria use to detoxify their cytosol through the uptake of reactive iron species. In the stationary growth phase of bacteria, Dps enzymes are primarily used to protect DNA by biocrystallization. To characterize the wild type Dps protein from Microbacterium arborescens that displays additional catalytic functions (amide hydrolysis and synthesis), we determined the crystal structure to a resolution of 2.05 Å at low iron content. The structure shows a single iron at the ferroxidase center coordinated by an oxo atom, one water molecule, and three ligating residues. An iron-enriched protein structure was obtained at 2 Å and shows the stepwise uptake of two hexahydrated iron atoms moving along channels at the 3-fold axis before a restriction site inside the channels requires removal of the hydration sphere. Supporting biochemical data provide insight into the regulation of this acylamino acid hydrolase. Moreover, the peroxidase activity of the protein was determined. The influence of iron and siderophores on the expression of acylamino acid hydrolase was monitored during several stages of cell growth. Altogether our data provide an interesting view of an unusual Dps-like enzyme evolutionarily located apart from the large Dps sequence clusters.
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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.