4OI6
Crystal structure analysis of nickel-bound form SCO4226 from Streptomyces coelicolor A3(2)
Summary for 4OI6
| Entry DOI | 10.2210/pdb4oi6/pdb |
| Related | 4OI3 |
| Descriptor | Nickel responsive protein, NICKEL (II) ION, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | nickel responsive protein, structural genomics, ferredoxin-like fold, a nickel responsive protein, nickel binding, metal binding protein |
| Biological source | Streptomyces coelicolor |
| Total number of polymer chains | 2 |
| Total formula weight | 20850.10 |
| Authors | Lu, M.,Jiang, Y.L.,Wang, S.,Cheng, W.,Zhang, R.G.,Virolle, M.J.,Chen, Y.,Zhou, C.Z. (deposition date: 2014-01-18, release date: 2014-09-10, Last modification date: 2024-10-16) |
| Primary citation | Lu, M.,Jiang, Y.L.,Wang, S.,Jin, H.,Zhang, R.G.,Virolle, M.J.,Chen, Y.,Zhou, C.Z. Streptomyces coelicolor SCO4226 Is a Nickel Binding Protein. Plos One, 9:e109660-e109660, 2014 Cited by PubMed Abstract: 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 Å resolution, respectively. Each subunit of SCO4226 dimer adopts a canonical ferredoxin-like fold with five β-strands flanked by two α-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. PubMed: 25285530DOI: 10.1371/journal.pone.0109660 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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