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PDBsum entry 2mrb
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Metallothionein
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PDB id
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2mrb
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional structure of rabbit liver [cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance.
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Authors
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A.Arseniev,
P.Schultze,
E.Wörgötter,
W.Braun,
G.Wagner,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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J Mol Biol, 1988,
201,
637-657.
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PubMed id
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Abstract
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In previous work the metal-polypeptide co-ordinative bonds in the major protein
species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit
liver in aqueous solution were determined, the secondary polypeptide structure
was found to contain several half-turns and 3(10)-helical segments, and a
preliminary characterization of the overall polypeptide backbone fold in the
beta-domain containing the three-metal cluster, and the alpha-domain containing
the four-metal cluster, was obtained. Using a new, more extensive set of nuclear
magnetic resonance data these earlier structures were improved by new structure
calculations. The new experimental data consist of distance constraints from
measurements of nuclear Overhauser effects, and dihedral angle constraints
derived from both coupling constants and nuclear Overhauser effects. The
structure calculations were performed with the program DISMAN. Since no
information on the orientation of the two domains relative to each other could
be obtained, the structure calculations were performed separately for the
alpha-domain and the beta-domain. The average of the pairwise root-mean-square
distances among the 20 structures with the least residual violations of input
constraints was 2.9 A for the beta-domain and 1.4 A for the alpha-domain (1 A =
0.1 nm). The overall chirality of the polypeptide fold is right-handed for the
beta-domain and left-handed for the alpha-domain. For each of the seven metal
ions the local chirality of the co-ordination of the four cysteinyl Sy atoms is
clearly defined. The improved structures of both domains show the previously
noted differences relative to the recently published crystal structure of
metallothionein-2a from rat liver.
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Secondary reference #1
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Title
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Nuclear magnetic resonance identification of "half-Turn" and 3(10)-Helix secondary structure in rabbit liver metallothionein-2.
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Authors
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G.Wagner,
D.Neuhaus,
E.Wörgötter,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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J Mol Biol, 1986,
187,
131-135.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. pectral region containing the amide rotoll-cc-proton crosspeaks from a phase-sensitive SOESY spectrum
f a 0.01 solution of MT-2 in ater (pH 7.0) at 14°C. recorded ith mixing t,ime of' s. As a llustration of the
pectral analysis. some sequential and medium-range NOES d,,. d,,(i,i+2) and d,,(i.i+3) used or t,he econdar)
tructure determnation (Fig. 3(d)) are identifid by the equence I'ositions of the interacting pins. or reference
urposes. ome intraresidue K'OEs, d&i, ave also been identified. p.p.m.. parts per million.
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Figure 3.
Figure 3. (a) lVOE atterns an pin-spin ouplings 3JnN. expected or the tandard f n cc-helix. a
Y,,-helix. ight urns f the types I I. I' and II', and alf-turns. The numeration at he ottom refers to he amino cid
residues contained n the secondary tructure lements and 3JnN, s ndicated immediatelv above these umbers, Short
HP'H istances btween 2 esidues are indicated by bars, here the thickness s roportional to -6. b) Survev of the
exerimental data or T-2. In emi-quantitative nalysis f he NOESY pectra. he NOES ere classified as
``strong'' or ``weak''. which is epresented by heavy or ight lines, respectively. The alues for JHNz are indicated
immediately above the sequence, where indicates that 3JnN, 5 7 z. he locations f alf-turn h) ad ,,-helical
secondary structures 3,,) re ndicated above he equence. The filled ircle for the structure element from esidues 38
to 41 indicates hat this could either be a type II tight' turn or half-turn.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution.
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Authors
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W.Braun,
G.Wagner,
E.Wörgötter,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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J Mol Biol, 1986,
187,
125-129.
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PubMed id
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Secondary reference #3
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Title
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Sequence-Specific 1h-Nmr assignments in rabbit-Liver metallothionein-2.
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Authors
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G.Wagner,
D.Neuhaus,
E.Wörgötter,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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Eur J Biochem, 1986,
157,
275-289.
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PubMed id
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Secondary reference #4
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Title
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Systematic application of high-Resolution, Phase-Sensitive two-Dimensional 1h-Nmr techniques for the identification of the amino-Acid-Proton spin systems in proteins. Rabbit metallothionein-2.
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Authors
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D.Neuhaus,
G.Wagner,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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Eur J Biochem, 1985,
151,
257-273.
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PubMed id
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Secondary reference #5
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Title
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Polypeptide-Metal cluster connectivies in metallo thionein 2 by novel 1h-113cd heteronuclear two-Dimensional NMR experiments
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Authors
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M.H.Frey,
G.Wagner,
M.Vasak,
O.W.Sorensen,
D.Neuhaus,
E.Woergoetter,
J.H.R.Kaegi,
R.R.Ernst,
K.Wuthrich.
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Ref.
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j am chem soc, 1985,
107,
6847.
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