Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA. Banci, L., Bertini, I., Ciofi-Baffoni, S., Su, X., Miras, R., Bal, N., Mintz, E., Catty, P., Shokes, J. E, & Scott, R. A Journal of Molecular Biology, 356(3):638--650, February, 2006. ![Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex In bacteria, P1-type ATPases are responsible for resistance to di- and monovalent toxic heavy metals by taking them out of the cell. These ATPases have a cytoplasmic N terminus comprising metal binding domains defined by a betaalphabetabetaalphabeta fold and a CXXC metal binding motif. To check how the structural properties of the metal binding site in the N terminus can influence the metal specificity of the ATPase, the first structure of a Cd(II)-ATPase N terminus was determined by NMR and its coordination sphere was investigated by X-ray absorption spectroscopy. A novel metal binding environment was found, comprising the two conserved Cys residues of the metal binding motif and a Glu in loop 5. A bioinformatic search identifies an ensemble of highly homologous sequences presumably with the same function. Another group of highly homologous sequences is found which can be referred to as zinc-detoxifying P1-type ATPases with the metal binding pattern DCXXC in the N terminus. Because no carboxylate groups participate in Cu(I) or Ag(I) binding sites, we suggest that the acidic residue plays a key role in the coordination properties of divalent cations, hence conferring a function to the N terminus in the metal specificity of the ATPase.
@article{banci_structural_2006,
title = {Structural basis for metal binding specificity: the {N}-terminal cadmium binding domain of the {P}1-type {ATPase} {CadA}},
volume = {356},
issn = {0022-2836},
shorttitle = {Structural basis for metal binding specificity},
url = {http://www.ncbi.nlm.nih.gov/pubmed/16388822},
doi = {10.1016/j.jmb.2005.11.055},
abstract = {In bacteria, P1-type ATPases are responsible for resistance to di- and monovalent toxic heavy metals by taking them out of the cell. These ATPases have a cytoplasmic N terminus comprising metal binding domains defined by a betaalphabetabetaalphabeta fold and a CXXC metal binding motif. To check how the structural properties of the metal binding site in the N terminus can influence the metal specificity of the ATPase, the first structure of a Cd(II)-ATPase N terminus was determined by NMR and its coordination sphere was investigated by X-ray absorption spectroscopy. A novel metal binding environment was found, comprising the two conserved Cys residues of the metal binding motif and a Glu in loop 5. A bioinformatic search identifies an ensemble of highly homologous sequences presumably with the same function. Another group of highly homologous sequences is found which can be referred to as zinc-detoxifying P1-type ATPases with the metal binding pattern DCXXC in the N terminus. Because no carboxylate groups participate in Cu(I) or Ag(I) binding sites, we suggest that the acidic residue plays a key role in the coordination properties of divalent cations, hence conferring a function to the N terminus in the metal specificity of the ATPase.},
number = {3},
urldate = {2009-10-31TZ},
journal = {Journal of Molecular Biology},
author = {Banci, Lucia and Bertini, Ivano and Ciofi-Baffoni, Simone and Su, Xun-Cheng and Miras, Roger and Bal, Nathalie and Mintz, Elisabeth and Catty, Patrice and Shokes, Jacob E and Scott, Robert A},
month = feb,
year = {2006},
pmid = {16388822},
keywords = {Adenosine Triphosphatases, Amino Acid Sequence, Apoenzymes, Biological Transport, Active, Cadmium, Cation Transport Proteins, Cations, Divalent, Crystallography, X-Ray, Dimerization, Escherichia coli, Listeria monocytogenes, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Solutions, Thermodynamics},
pages = {638--650}
}
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To check how the structural properties of the metal binding site in the N terminus can influence the metal specificity of the ATPase, the first structure of a Cd(II)-ATPase N terminus was determined by NMR and its coordination sphere was investigated by X-ray absorption spectroscopy. A novel metal binding environment was found, comprising the two conserved Cys residues of the metal binding motif and a Glu in loop 5. A bioinformatic search identifies an ensemble of highly homologous sequences presumably with the same function. Another group of highly homologous sequences is found which can be referred to as zinc-detoxifying P1-type ATPases with the metal binding pattern DCXXC in the N terminus. 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