Structural highlights
Publication Abstract from PubMed
The open reading frame SCO4226 of Streptomyces coelicolor A3(2) encodes an 82-residue hypothetical protein. Biochemical assays revealed that each SCO4226 dimer binds four nickel ions. To decipher the molecular function, we solved the crystal structures of SCO4226 in both apo- and nickel-bound (Ni-SCO4226) forms at 1.30 and 2.04 A resolution, respectively. Each subunit of SCO4226 dimer adopts a canonical ferredoxin-like fold with five beta-strands flanked by two alpha-helices. In the structure of Ni-SCO4226, four nickel ions are coordinated at the surface of the dimer. Further biochemical assays suggested that the binding of Ni2+ triggers the self-aggregation of SCO4226 in vitro. In addition, RT-qPCR assays demonstrated that the expression of SCO4226 gene in S. coelicolor is specifically up-regulated by the addition of Ni2+, but not other divalent ions such as Cu2+, Mn2+ or Co2+. All these results suggested that SCO4226 acts as a nickel binding protein, probably required for nickel sequestration and/or detoxification.
Streptomyces coelicolor SCO4226 Is a Nickel Binding Protein.,Lu M, Jiang YL, Wang S, Jin H, Zhang RG, Virolle MJ, Chen Y, Zhou CZ PLoS One. 2014 Oct 6;9(10):e109660. doi: 10.1371/journal.pone.0109660., eCollection 2014. PMID:25285530[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu M, Jiang YL, Wang S, Jin H, Zhang RG, Virolle MJ, Chen Y, Zhou CZ. Streptomyces coelicolor SCO4226 Is a Nickel Binding Protein. PLoS One. 2014 Oct 6;9(10):e109660. doi: 10.1371/journal.pone.0109660., eCollection 2014. PMID:25285530 doi:http://dx.doi.org/10.1371/journal.pone.0109660
