 |
PDBsum entry 1fvq
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure of the yeast copper transporter domain ccc2a in the apo and cu(i)-Loaded states.
|
|
|
Authors
|
|
L.Banci,
I.Bertini,
S.Ciofi-Baffoni,
D.L.Huffman,
T.V.O'Halloran.
|
|
|
Ref.
|
|
J Biol Chem, 2001,
276,
8415-8426.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
