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PDBsum entry 1ix2
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Metal binding protein
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PDB id
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1ix2
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Metal binding protein
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Title:
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Crystal structure of selenomethionine pcoc, a copper resistance protein from escherichia coli
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Structure:
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Pcoc copper resistance protein. Chain: a, b. Synonym: copper resistance protein c. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: plasmid prj1004. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Hexamer (from
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Resolution:
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1.55Å
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R-factor:
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0.207
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R-free:
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0.228
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Authors:
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A.K.Wernimont,D.L.Huffman,L.A.Finney,B.Demeler,T.V.O'Halloran, A.C.Rosenzweig
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Key ref:
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A.K.Wernimont
et al.
(2003).
Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli.
J Biol Inorg Chem,
8,
185-194.
PubMed id:
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Date:
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10-Jun-02
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Release date:
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27-Nov-02
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PROCHECK
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Headers
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References
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Q47454
(PCOC_ECOLX) -
Copper resistance protein C from Escherichia coli
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Seq:
Struc:
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126 a.a.
102 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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J Biol Inorg Chem
8:185-194
(2003)
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PubMed id:
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Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli.
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A.K.Wernimont,
D.L.Huffman,
L.A.Finney,
B.Demeler,
T.V.O'Halloran,
A.C.Rosenzweig.
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ABSTRACT
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PcoC is a soluble periplasmic protein encoded by the plasmid-born pco copper
resistance operon of Escherichia coli. Like PcoA, a multicopper oxidase encoded
in the same locus and its chromosomal homolog CueO, PcoC contains unusual
methionine rich sequences. Although essential for copper resistance, the
functions of PcoC, PcoA, and their conserved methionine-rich sequences are not
known. Similar methionine motifs observed in eukaryotic copper transporters have
been proposed to bind copper, but there are no precedents for such metal binding
sites in structurally characterized proteins. The high-resolution structures of
apo PcoC, determined for both the native and selenomethionine-containing
proteins, reveal a seven-stranded beta barrel with the methionines unexpectedly
housed on a solvent-exposed loop. Several potential metal-binding sites can be
discerned by comparing the structures to spectroscopic data reported for
copper-loaded PcoC. In the native structure, the methionine loop interacts with
the same loop on a second molecule in the asymmetric unit. In the
selenomethionine structure, the methionine loops are more exposed, forming
hydrophobic patches on the protein surface. These two arrangements suggest that
the methionine motifs might function in protein-protein interactions between
PcoC molecules or with other methionine-rich proteins such as PcoA. Analytical
ultracentrifugation data indicate that a weak monomer-dimer equilibrium exists
in solution for the apo protein. Dimerization is significantly enhanced upon
binding Cu(I) with a measured delta(deltaG degrees )<or=-8.0 kJ/mole,
suggesting that copper might bind at the dimer interface.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.T.Rubino,
P.Riggs-Gelasco,
and
K.J.Franz
(2010).
Methionine motifs of copper transport proteins provide general and flexible thioether-only binding sites for Cu(I) and Ag(I).
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J Biol Inorg Chem,
15,
1033-1049.
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Z.Xiao,
and
A.G.Wedd
(2010).
The challenges of determining metal-protein affinities.
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Nat Prod Rep,
27,
768-789.
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A.K.Boal,
and
A.C.Rosenzweig
(2009).
Structural biology of copper trafficking.
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Chem Rev,
109,
4760-4779.
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Z.Ma,
F.E.Jacobsen,
and
D.P.Giedroc
(2009).
Coordination chemistry of bacterial metal transport and sensing.
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Chem Rev,
109,
4644-4681.
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K.Y.Djoko,
Z.Xiao,
and
A.G.Wedd
(2008).
Copper resistance in E. coli: the multicopper oxidase PcoA catalyzes oxidation of copper(I) in Cu(I)Cu(II)-PcoC.
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Chembiochem,
9,
1579-1582.
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S.C.Drew,
K.Y.Djoko,
L.Zhang,
M.Koay,
J.F.Boas,
J.R.Pilbrow,
Z.Xiao,
K.J.Barnham,
and
A.G.Wedd
(2008).
Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli.
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J Biol Inorg Chem,
13,
899-907.
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A.S.Hakemian,
and
A.C.Rosenzweig
(2007).
The biochemistry of methane oxidation.
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Annu Rev Biochem,
76,
223-241.
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C.Singleton,
and
N.E.Le Brun
(2007).
Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer.
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Biometals,
20,
275-289.
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D.Quaranta,
R.McCarty,
V.Bandarian,
and
C.Rensing
(2007).
The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a pre-Q0 reductase in Pseudomonas putida KT2440.
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J Bacteriol,
189,
5361-5371.
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A.Láng,
I.G.Csizmadia,
and
A.Perczel
(2005).
Peptide models XLV: conformational properties of N-formyl-L-methioninamide and its relevance to methionine in proteins.
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Proteins,
58,
571-588.
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L.Banci,
I.Bertini,
S.Ciofi-Baffoni,
E.Katsari,
N.Katsaros,
K.Kubicek,
and
S.Mangani
(2005).
A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.
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Proc Natl Acad Sci U S A,
102,
3994-3999.
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PDB codes:
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C.Rensing,
and
G.Grass
(2003).
Escherichia coli mechanisms of copper homeostasis in a changing environment.
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FEMS Microbiol Rev,
27,
197-213.
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H.B.Gray
(2003).
Biological inorganic chemistry at the beginning of the 21st century.
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Proc Natl Acad Sci U S A,
100,
3563-3568.
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L.A.Finney,
and
T.V.O'Halloran
(2003).
Transition metal speciation in the cell: insights from the chemistry of metal ion receptors.
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Science,
300,
931-936.
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S.A.Roberts,
G.F.Wildner,
G.Grass,
A.Weichsel,
A.Ambrus,
C.Rensing,
and
W.R.Montfort
(2003).
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO.
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J Biol Chem,
278,
31958-31963.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
