1ON4
Solution structure of soluble domain of Sco1 from Bacillus Subtilis
Summary for 1ON4
| Entry DOI | 10.2210/pdb1on4/pdb |
| NMR Information | BMRB: 5742 |
| Descriptor | Sco1 (1 entity in total) |
| Functional Keywords | cox assembly protein, copper protein, sco1 from b. subtilis, thioredoxin-like fold, ypmq, structural proteomics in europe, spine, structural genomics, metal binding protein |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side: P54178 |
| Total number of polymer chains | 1 |
| Total formula weight | 19856.35 |
| Authors | Balatri, E.,Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S.,Structural Proteomics in Europe (SPINE) (deposition date: 2003-02-27, release date: 2003-11-11, Last modification date: 2024-05-29) |
| Primary citation | Balatri, E.,Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S. Solution Structure of Sco1: A Thioredoxin-like Protein Involved in Cytochrome c Oxidase Assembly STRUCTURE, 11:1431-1433, 2003 Cited by PubMed Abstract: Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single transmembrane segment. The solution structure of the soluble part of apoSco1 from Bacillus subtilis has been solved by NMR and the internal mobility characterized. Its fold places Sco1 in a distinct subgroup of the functionally unrelated thioredoxin proteins. In vitro Sco1 binds copper(I) through a CXXXCP motif and possibly His 135 and copper(II) in two different species, thus suggesting that copper(II) is adventitious more than physiological. The Sco1 structure represents the first structure of this class of proteins, present in a variety of eukaryotic and bacterial organisms, and elucidates a link between copper trafficking proteins and thioredoxins. The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family. PubMed: 14604533DOI: 10.1016/j.str.2003.10.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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