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PDBsum entry 1p6t
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural basis for the function of the n-Terminal domain of the atpase copa from bacillus subtilis.
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Authors
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L.Banci,
I.Bertini,
S.Ciofi-Baffoni,
L.Gonnelli,
X.C.Su.
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Ref.
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J Biol Chem, 2003,
278,
50506-50513.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
50506-50513)
copyright 2003.
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