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Helical copper-binding motif

Fig. 3. Comparison of the membrane topology of a CPx-type ATPase and a nonheavy metal ATPase. Shown are CopB of Enterococcus hirae and the Ca -ATPase of sarcoplasmic reticnlnm. Helices common to both types of ATPases are in gray and helices nniqne to one type of ATPase are in black. Key seqnence motifs are indicated in single-letter amino acid code. In the center of the hgnre, the approximate locations of the three cytoplasmic domains. A, P, and N, are indicated. MBD, metal-binding domain containing repeat metal-binding sites TGE, conserved site in transdnction domain (A) CPx, pntative copper-binding site DKTGT, phosphorylation site in domain P HP, motif of nnknown function, probably in domain N GDG, nucleotide-binding site residues in domain N. Fig. 3. Comparison of the membrane topology of a CPx-type ATPase and a nonheavy metal ATPase. Shown are CopB of Enterococcus hirae and the Ca -ATPase of sarcoplasmic reticnlnm. Helices common to both types of ATPases are in gray and helices nniqne to one type of ATPase are in black. Key seqnence motifs are indicated in single-letter amino acid code. In the center of the hgnre, the approximate locations of the three cytoplasmic domains. A, P, and N, are indicated. MBD, metal-binding domain containing repeat metal-binding sites TGE, conserved site in transdnction domain (A) CPx, pntative copper-binding site DKTGT, phosphorylation site in domain P HP, motif of nnknown function, probably in domain N GDG, nucleotide-binding site residues in domain N.

See other pages where Helical copper-binding motif is mentioned: [Pg.83]    [Pg.83]    [Pg.241]    [Pg.314]    [Pg.113]    [Pg.236]    [Pg.773]    [Pg.326]    [Pg.98]    [Pg.10]    [Pg.125]   
See also in sourсe #XX -- [ Pg.83 ]




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Binding motifs

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