PDBsum entry 2aj1

Hydrolase

PDB id: 2aj1

Contents

Protein chain

71 a.a. *

* Residue conservation analysis

PDB id:

2aj1

Name:

Hydrolase

Title:

Solution structure of apocada

Structure:

Probable cadmium-transporting atpase. Chain: a. Fragment: n-terminal domain. Synonym: cada p-type atpase, cadmium efflux atpase. Engineered: yes. Mutation: yes

Source:

Listeria monocytogenes. Organism_taxid: 1639. Gene: cada. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

L.Banci,I.Bertini,S.Ciofi-Baffoni,X.-C.Su,R.Miras,N.Bal,E.Mintz, P.Catty,J.E.Shokes,R.A.Scott

Key ref:

L.Banci et al. (2006). Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA. J Mol Biol, 356, 638-650. PubMed id: 16388822 DOI: 10.1016/j.jmb.2005.11.055

Date:

01-Aug-05 Release date: 02-May-06

Protein chain

Q60048  (CADA_LISMN) -  Probable cadmium-transporting ATPase from Listeria monocytogenes

Seq: 711 a.a.

Struc: 71 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.7.2.2.21 - Cd(2+)-exporting ATPase.
• Reaction: Cd²⁺(in) + ATP + H2O = Cd²⁺(out) + ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jmb.2005.11.055

J Mol Biol 356:638-650 (2006)

PubMed id: 16388822

Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA.

L.Banci, I.Bertini, S.Ciofi-Baffoni, X.C.Su, R.Miras, N.Bal, E.Mintz, P.Catty, J.E.Shokes, R.A.Scott.

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.

Selected figure(s)

Figure 5.
Figure 5. (a) Cd K edge spectra and (b) Fourier transforms (k3 weighting, k=2-13 Å -1) for CadA NTKII (continuous) and CadA NTKII+TCEP (broken). k3-weighted EXAFS data are presented in the inset to (b).

Figure 7.
Figure 7. Solution structures of N-terminal metal-binding domains of L. monocytogenes CadA, E. coli ZntA (1MWY) and B. subtilis CopA (1JWW). Apo forms of the proteins, marked with an asterisk in Figure 3, are compared here. van der Waals contacts involving some hydrophobic residues are shown in blue, the metal ligands are shown in yellow and some highly conserved residues are in red. The Gly residues, shaded in cyan in Figure 3, are mapped in cyan on the backbone of the structures.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 356, 638-650) copyright 2006.

Figures were selected by an automated process.