PDBsum entry 1p6t

Hydrolase

PDB id: 1p6t

Contents

Protein chain

151 a.a. *

* Residue conservation analysis

PDB id:

1p6t

Name:

Hydrolase

Title:

Structure characterization of the water soluble region of p-type atpase copa from bacillus subtilis

Structure:

Potential copper-transporting atpase. Chain: a. Fragment: n-terminal water soluble region (residues 1-147). Engineered: yes. Mutation: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: yvgx. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

L.Banci,I.Bertini,S.Ciofi-Baffoni,L.Gonnelli,X.C.Su,Structural Proteomics In Europe (Spine)

Key ref:

L.Banci et al. (2003). Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis. J Biol Chem, 278, 50506-50513. PubMed id: 14514665 DOI: 10.1074/jbc.M307389200

Date:

30-Apr-03 Release date: 16-Dec-03

Protein chain

O32220  (COPA_BACSU) -  Copper-exporting P-type ATPase from Bacillus subtilis (strain 168)

Seq: 802 a.a.

Struc: 151 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.7.2.2.8 - P-type Cu(+) transporter.
• Reaction: Cu⁺(in) + ATP + H2O = Cu⁺(out) + ADP + phosphate + H⁺

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

reference

DOI no: 10.1074/jbc.M307389200

J Biol Chem 278:50506-50513 (2003)

PubMed id: 14514665

Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.

L.Banci, I.Bertini, S.Ciofi-Baffoni, L.Gonnelli, X.C.Su.

ABSTRACT

The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases.

Selected figure(s)

Figure 2.
FIG. 2. 30 lowest energy structures of apoCopAab (residues 3-144) from B. subtilis, shown as a tube with a radius proportional to the backbone r.m.s.d. value of each residue. 3[10]-helix and -helices are in black, and -strands are in white.

Figure 6.
FIG. 6. Electrostatic potential surfaces of apoCopAab orientated in such a way to show the copper binding sites. The positively and negatively charged and neutral amino acids are represented in blue, red, and white, respectively. The Cys ligands are also shown in yellow.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 50506-50513) copyright 2003.

Figures were selected by an automated process.