2AJ0

Solution structure of apoCadA

Summary for 2AJ0

• Entry DOI: 10.2210/pdb2aj0/pdb
• Related: 2AJ1
• NMR Information: BMRB: 6811
• Descriptor: Probable cadmium-transporting ATPase (1 entity in total)
• Functional Keywords: ferrodoxin-like fold, beta-alpha-beta-beta-alpha-beta, metal binding protein, hydrolase
• Biological source: Listeria monocytogenes
• Cellular location: Cell membrane; Multi-pass membrane protein: Q60048
• Total number of polymer chains: 1
• Total formula weight: 7708.73

Authors

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Su, X.-C.,Miras, R.,Bal, N.,Mintz, E.,Catty, P.,Shokes, J.E.,Scott, R.A. (deposition date: 2005-08-01, release date: 2006-05-02, Last modification date: 2024-05-29)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Su, X.-C.,Miras, R.,Bal, N.,Mintz, E.,Catty, P.,Shokes, J.E.,Scott, R.A.
Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA
J.Mol.Biol., 356:638-650, 2006

PubMed 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.

PubMed: 16388822
DOI: 10.1016/j.jmb.2005.11.055

Experimental method

SOLUTION NMR