1on4

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|ACTIVITY=
|ACTIVITY=
|GENE= YPMQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|GENE= YPMQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1on4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1on4 OCA], [http://www.ebi.ac.uk/pdbsum/1on4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1on4 RCSB]</span>
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[[Category: ypmq]]
[[Category: ypmq]]
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Revision as of 19:47, 30 March 2008


PDB ID 1on4

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Gene: YPMQ (Bacillus subtilis)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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