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PDBsum entry 1mrt
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Metallothionein
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PDB id
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1mrt
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J Mol Biol
203:251-268
(1988)
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PubMed id:
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Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy.
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P.Schultze,
E.Wörgötter,
W.Braun,
G.Wagner,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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ABSTRACT
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The three-dimensional structure of [Cd7]-metallothionein-2 from rat liver was
determined in aqueous solution, using nuclear magnetic resonance spectrometry
and distance geometry calculations. The experimental data provided proton-proton
distance constraints from measurements of nuclear Overhauser effects,
constraints on the geometry of the metal-cysteine clusters determined by
heteronuclear correlation spectroscopy, and dihedral angle constraints derived
from both coupling constants and nuclear Overhauser effects. The structure
calculations were performed with the program DISMAN. As in previous studies with
rabbit liver metallothionein-2a, the structure calculations were performed
separately for the alpha and beta-domains containing the 4 and 3-metal clusters,
respectively, since no interdomain constraints were found. For both domains, the
global polypeptide fold, the location of polypeptide secondary structure
elements, the architecture of the metal-sulfur cluster and the local chirality
of the metal co-ordination are very similar to the solution structure of rabbit
metallothionein-2a, but show considerable difference relative to the crystal
structure of rat metallothionein-2.
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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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D.E.Sutherland,
and
M.J.Stillman
(2011).
The "magic numbers" of metallothionein.
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Metallomics,
3,
444-463.
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N.Romero-Isart,
B.Oliva,
and
M.Vasák
(2010).
Influence of NH-Sgamma bonding interactions on the structure and dynamics of metallothioneins.
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J Mol Model,
16,
387-394.
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G.Digilio,
C.Bracco,
L.Vergani,
M.Botta,
D.Osella,
and
A.Viarengo
(2009).
The cadmium binding domains in the metallothionein isoform Cd(7)-MT10 from Mytilus galloprovincialis revealed by NMR spectroscopy.
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J Biol Inorg Chem,
14,
167-178.
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H.Wang,
H.Li,
B.Cai,
Z.X.Huang,
and
H.Sun
(2008).
The effect of nitric oxide on metal release from metallothionein-3: gradual unfolding of the protein.
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J Biol Inorg Chem,
13,
411-419.
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F.Y.Ni,
B.Cai,
Z.C.Ding,
F.Zheng,
M.J.Zhang,
H.M.Wu,
H.Z.Sun,
and
Z.X.Huang
(2007).
Structural prediction of the beta-domain of metallothionein-3 by molecular dynamics simulation.
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Proteins,
68,
255-266.
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E.Casero,
J.A.Martín-Gago,
F.Pariente,
and
E.Lorenzo
(2004).
Metal release in metallothioneins induced by nitric oxide: X-ray absorption spectroscopy study.
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Eur Biophys J,
33,
726-731.
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L.Khatai,
W.Goessler,
H.Lorencova,
and
K.Zangger
(2004).
Modulation of nitric oxide-mediated metal release from metallothionein by the redox state of glutathione in vitro.
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Eur J Biochem,
271,
2408-2416.
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P.A.Cobine,
R.T.McKay,
K.Zangger,
C.T.Dameron,
and
I.M.Armitage
(2004).
Solution structure of Cu6 metallothionein from the fungus Neurospora crassa.
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Eur J Biochem,
271,
4213-4221.
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PDB code:
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R.Jin,
J.Huang,
P.H.Tan,
and
B.H.Bay
(2004).
Clinicopathological significance of metallothioneins in breast cancer.
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Pathol Oncol Res,
10,
74-79.
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C.A.Blindauer,
M.D.Harrison,
J.A.Parkinson,
A.K.Robinson,
J.S.Cavet,
N.J.Robinson,
and
P.J.Sadler
(2001).
A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity.
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Proc Natl Acad Sci U S A,
98,
9593-9598.
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PDB code:
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E.Smyth,
C.D.Syme,
E.W.Blanch,
L.Hecht,
M.Vasák,
and
L.D.Barron
(2001).
Solution structure of native proteins with irregular folds from Raman optical activity.
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Biopolymers,
58,
138-151.
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C.D.Berweger,
W.Thiel,
and
W.F.van Gunsteren
(2000).
Molecular-dynamics simulation of the beta domain of metallothionein with a semi-empirical treatment of the metal core.
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Proteins,
41,
299-315.
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H.Sun,
H.Li,
I.Harvey,
and
P.J.Sadler
(1999).
Interactions of bismuth complexes with metallothionein(II).
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J Biol Chem,
274,
29094-29101.
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K.Zangger,
G.Oz,
J.D.Otvos,
and
I.M.Armitage
(1999).
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy.
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Protein Sci,
8,
2630-2638.
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PDB codes:
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J.Zaia,
D.Fabris,
D.Wei,
R.L.Karpel,
and
C.Fenselau
(1998).
Monitoring metal ion flux in reactions of metallothionein and drug-modified metallothionein by electrospray mass spectrometry.
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Protein Sci,
7,
2398-2404.
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D.Bentrop,
I.Bertini,
F.Capozzi,
A.Dikiy,
L.Eltis,
and
C.Luchinat
(1996).
Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type protein.
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Biochemistry,
35,
5928-5936.
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PDB code:
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J.Zaia,
L.Jiang,
M.S.Han,
J.R.Tabb,
Z.Wu,
D.Fabris,
and
C.Fenselau
(1996).
A binding site for chlorambucil on metallothionein.
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Biochemistry,
35,
2830-2835.
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R.Bogumil,
P.Faller,
D.L.Pountney,
and
M.Vasák
(1996).
Evidence for Cu(I) clusters and Zn(II) clusters in neuronal growth-inhibitory factor isolated from bovine brain.
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Eur J Biochem,
238,
698-705.
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I.Bertini,
I.C.Felli,
D.H.Kastrau,
C.Luchinat,
M.Piccioli,
and
M.S.Viezzoli
(1994).
Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.
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Eur J Biochem,
225,
703-714.
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X.Q.Ding,
C.Butzlaff,
E.Bill,
D.L.Pountney,
G.Henkel,
H.Winkler,
M.Vasák,
and
A.X.Trautwein
(1994).
Mössbauer and magnetic susceptibility studies on iron(II) metallothionein from rabbit liver. Evidence for the existence of an unusual type of [M3(CysS)9]3- cluster.
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Eur J Biochem,
220,
827-837.
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Y.Wang,
E.A.Mackay,
M.Kurasaki,
and
J.H.Kägi
(1994).
Purification and characterisation of recombinant sea urchin metallothionein expressed in Escherichia coli.
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Eur J Biochem,
225,
449-457.
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I.Bertini,
C.Luchinat,
L.Messori,
and
M.Vasak
(1993).
A two-dimensional NMR study of Co(II)7 rabbit liver metallothionein.
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Eur J Biochem,
211,
235-240.
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M.W.MacArthur,
and
J.M.Thornton
(1993).
Conformational analysis of protein structures derived from NMR data.
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Proteins,
17,
232-251.
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D.L.Pountney,
and
M.Vasák
(1992).
Spectroscopic studies on metal distribution in Co(II)/Zn(II) mixed-metal clusters in rabbit liver metallothionein 2.
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Eur J Biochem,
209,
335-341.
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L.A.Basile,
and
J.E.Coleman
(1992).
Optical activity associated with the sulfur to metal charge transfer bands of Zn and Cd GAL4.
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Protein Sci,
1,
617-624.
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M.Billeter
(1992).
Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
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Q Rev Biophys,
25,
325-377.
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P.Palumaa,
and
M.Vasák
(1992).
Binding of inorganic phosphate to the cadmium-induced dimeric form of metallothionein from rabbit liver.
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Eur J Biochem,
205,
1131-1135.
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W.Braun,
M.Vasák,
A.H.Robbins,
C.D.Stout,
G.Wagner,
J.H.Kägi,
and
K.Wüthrich
(1992).
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
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Proc Natl Acad Sci U S A,
89,
10124-10128.
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PDB code:
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B.L.Vallee,
J.E.Coleman,
and
D.S.Auld
(1991).
Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains.
|
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Proc Natl Acad Sci U S A,
88,
999.
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M.Good,
R.Hollenstein,
and
M.Vasák
(1991).
Metal selectivity of clusters in rabbit liver metallothionein.
|
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Eur J Biochem,
197,
655-659.
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M.L.Chernaik,
and
P.C.Huang
(1991).
Differential effect of cysteine-to-serine substitutions in metallothionein on cadmium resistance.
|
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Proc Natl Acad Sci U S A,
88,
3024-3028.
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Y.Uchida,
K.Takio,
K.Titani,
Y.Ihara,
and
M.Tomonaga
(1991).
The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein.
|
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Neuron,
7,
337-347.
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G.Otting,
and
K.Wüthrich
(1990).
Heteronuclear filters in two-dimensional [1H,1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions.
|
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Q Rev Biophys,
23,
39-96.
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T.F.Havel
(1990).
The sampling properties of some distance geometry algorithms applied to unconstrained polypeptide chains: a study of 1830 independently computed conformations.
|
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Biopolymers,
29,
1565-1585.
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T.Pan,
and
J.E.Coleman
(1990).
GAL4 transcription factor is not a "zinc finger" but forms a Zn(II)2Cys6 binuclear cluster.
|
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Proc Natl Acad Sci U S A,
87,
2077-2081.
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G.M.Clore,
and
A.M.Gronenborn
(1989).
Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy.
|
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Crit Rev Biochem Mol Biol,
24,
479-564.
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J.H.Kägi,
and
P.Hunziker
(1989).
Mammalian metallothionein.
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Biol Trace Elem Res,
21,
111-118.
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M.Sanner,
A.Widmer,
H.Senn,
and
W.Braun
(1989).
GEOM: a new tool for molecular modelling based on distance geometry calculations with NMR data.
|
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J Comput Aided Mol Des,
3,
195-210.
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P.E.Wright
(1989).
What can two-dimensional NMR tell us about proteins?
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Trends Biochem Sci,
14,
255-260.
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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
code is
shown on the right.
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