PDBsum entry 1fvq

Hydrolase

PDB id: 1fvq

Contents

Protein chain

72 a.a. *

* Residue conservation analysis

PDB id:

1fvq

Name:

Hydrolase

Title:

Solution structure of the yeast copper transporter domain ccc2a in the apo and cu(i) loaded states

Structure:

Copper-transporting atpase. Chain: a. Fragment: ccc2a domain. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

L.Banci,I.Bertini,S.Ciofi Baffoni,D.L.Huffman,T.V.O'Halloran

Key ref:

L.Banci et al. (2001). Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J Biol Chem, 276, 8415-8426. PubMed id: 11083871 DOI: 10.1074/jbc.M008389200

Date:

20-Sep-00 Release date: 14-Mar-01

Protein chain

P38995  (ATU2_YEAST) -  Copper-transporting ATPase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1004 a.a.

Struc: 72 a.a.*

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

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.M008389200

J Biol Chem 276:8415-8426 (2001)

PubMed id: 11083871

Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states.

L.Banci, I.Bertini, S.Ciofi-Baffoni, D.L.Huffman, T.V.O'Halloran.

ABSTRACT

Ccc2 is an intracellular copper transporter in Saccharomyces cerevisiae and is a physiological target of the copper chaperone Atx1. Here we describe the solution structure of the first N-terminal MTCXXC metal-binding domain, Ccc2a, both in the presence and absence of Cu(I). For Cu(I)-Ccc2a, 1944 meaningful nuclear Overhauser effects were used to obtain a family of 35 structures with root mean square deviation to the average structure of 0.36 +/- 0.06 A for the backbone and 0.79 +/- 0.05 A for the heavy atoms. For apo-Ccc2a, 1970 meaningful nuclear Overhauser effects have been used with 35 (3)J(HNHalpha) to obtain a family of 35 structures with root mean square deviation to the average structure of 0.38 +/- 0.06 A for the backbone and 0.82 +/- 0.07 A for the heavy atoms. The protein exhibits a betaalphabetabetaalphabeta, ferrodoxin-like fold similar to that of its target Atx1 and that of a human counterpart, the fourth metal-binding domain of the Menkes protein. The overall fold remains unchanged upon copper loading, but the copper-binding site itself becomes less disordered. The helical context of the copper-binding site, and the copper-induced conformational changes in Ccc2a differ from those in Atx1. Ccc2a presents a conserved acidic surface which complements the basic surface of Atx1 and a hydrophobic surface. These results open new mechanistic aspects of copper transporter domains with physiological copper donor and acceptor proteins.

Selected figure(s)

Figure 2.
Fig. 2. Schematic representation of the sequential and medium range NOE connectivities involving NH, H , and H protons for apo-Ccc2a (A) and Cu(I)-Ccc2a (B). The thickness of the bar indicates the intensity of NOEs.

Figure 13.
Fig. 13. Electrostatic potential surface of the Cu(I)-Ccc2a (A), Ag(I)-mdb4 (B), and Cu(I)-Atx1 (C). The positively charged, negatively charged, and neutral amino acids are represented in blue, red, and white, respectively. Copper ion is represented in green, silver ion in teal, and cysteine sulfur in yellow. In A and C, the residues that might have a role in molecular recognition and copper transfer are indicated. In B, the negative residues that form a negative region close to metal binding loop are indicated. The figure was generated with the program MOLMOL (45).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 8415-8426) copyright 2001.

Figures were selected by an automated process.