1on4

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Revision as of 20:54, 20 November 2007

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Solution structure of soluble domain of Sco1 from Bacillus Subtilis

Overview

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.

About this Structure

1ON4 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

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

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