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. Author manuscript; available in PMC: 2014 Apr 15.
Published in final edited form as: Annu Rev Biochem. 2010;79:537–562. doi: 10.1146/annurev-biochem-030409-143539

Figure 5.

Figure 5

Copper metallochaperones for CcO. (a) Disulfide bonds between two pairs of cysteine residues (yellow) on antiparallel α-helices (red) create a helical hairpin of Cox17 [Protein Data Bank (PDB) code 2RNB]. Cu(I) is coordinated to a pair of cysteine residues. (b) Sco1 is tethered to the inner membrane (IM) (hydrophobic α-helix not shown) with a thioredoxin fold (β-strand, dark blue; histidine, pale blue) in the intermembrane space (PDB 2GQM). (c) Cox11 is tethered to the IM (hydrophobic α-helix not shown) with an immunoglobulin-like β-barrel in the IMS (PDB 1SPO).