Metallochaperones and Metal-Transporting ATPases: A Comparative Analysis of Sequences and Structures

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Figure 7.
Figure 7.

Sequence alignment of zinc- and cadmium-transporting ATPases. At the top, amino acid numbering is reported including gaps. The two metal-binding cysteines are shaded in blue. Some conserved negative (Glu and Asp) and positive (Arg and Lys) residues are indicated in red and blue, respectively. Positions where hydrophobic residues are conserved are highlighted in green. In column a we report sequence identity to Ccc2a from S. cerevisiae. 1gi‖586655 E. coli, strain K-12 (ZntA); 2gi‖15803981 E. coli, strain EDL-933; 3gi‖15641046 Vibrio cholerae; 4 gi‖2624376 P. mirabilis; 5 gi‖3123078 Synechocystis; 6gi‖15807741 D. radiodurans; 7 gi‖7436386 B. subtilis; 8 gi‖14521140 Pyrococcus abyssi;9 gi‖15789464 Halobacterium sp., strain NRC-1;10 gi‖10720043 H. felis; 11 gi‖15611794H. pylori, strain J99; 12 gi‖2493007 H. pylori, strain 26695; 13 gi‖79893 Staphylococcus aureus (CadA); 14 gi‖14020985 S. aureus II, 1st domain; 15 S. aureus II, 2nd domain; 16gi‖231677 Bacillus firmus; 17 gi‖15616598Bacillus halodurans; 18 gi‖3121832 Listeria monocytogenes; 19 gi‖9789448 L. lactis.

This Article

  1. Genome Res. 12: 255-271

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