1on4
Solution structure of soluble domain of Sco1 from Bacillus Subtilis
Structural highlights
FunctionSCO1_BACSU Neccessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSco1, 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. Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly.,Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S Structure. 2003 Nov;11(11):1431-43. PMID:14604533[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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