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Review
. 2013 Nov 27:3:89.
doi: 10.3389/fcimb.2013.00089. eCollection 2013.

Zinc and copper toxicity in host defense against pathogens: Mycobacterium tuberculosis as a model example of an emerging paradigm

Olivier Neyrolles  1 , Elisabeth Mintz  2 , Patrice Catty  2
Affiliations
Review

Zinc and copper toxicity in host defense against pathogens: Mycobacterium tuberculosis as a model example of an emerging paradigm

Olivier Neyrolles et al. Front Cell Infect Microbiol. .
No abstract available

Keywords: Mycobacterium tuberculosis; P-type ATPase; copper; macrophage; zinc.

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Figures

Figure 1
Figure 1
Main feature of M. tuberculosis P-type ATPases. (A) Sequences were aligned with ClustalW and organized in an unrooted tree using TreeView; *, indicates the presence of a gene that could encode a metallochaperone, upstream the P-type ATPase encoding gene. (B) Hydrophobicity profiles are shown for the 12 P-type M. tuberculosis ATPases. Sequences are aligned on the phosphorylation motif (encircled P in red); black squares represent membrane spanning helices. Ion-binding motifs in P1B-type ATPases: 1, Cys-X2-Cys; 2, (Cys/Ser/Ala)-Pro-Cys; 3, Ser-(Glu/Arg)-His-(Pro/Ser/Ala); 4, Met-X2-Ser-Ser, His-Glu-Gln-X-Thr. Ion-binding motifs in P2A-type ATPases: 2, Pro-Glu-Gly-(Leu/Met)-Pro; 5, Leu-Trp-X-Asn-X3-Asp. A domain: actuator domain; N domain: nucleotide-binding domain; P domain: phosphorylation motif. The method to identify transmembrane domains has been previously described (Kyte and Doolittle, 1982), and is accessible on the ExPASy website: http://web.expasy.org/protscale/. The analysis was performed using a 21-amino acid window.
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