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PDBsum entry 1msd
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Oxidoreductase (superoxide acceptor)
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PDB id
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1msd
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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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Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from thermus thermophilus: differences in dimer-Dimer interaction.
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Authors
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U.G.Wagner,
K.A.Pattridge,
M.L.Ludwig,
W.C.Stallings,
M.M.Werber,
C.Oefner,
F.Frolow,
J.L.Sussman.
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Ref.
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Protein Sci, 1993,
2,
814-825.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
97%.
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Abstract
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The three-dimensional X-ray structure of a recombinant human mitochondrial
manganese superoxide dismutase (MnSOD) (chain length 198 residues) was
determined by the method of molecular replacement using the related structure of
MnSOD from Thermus thermophilus as a search model. This tetrameric human MnSOD
crystallizes in space group P2(1)2(1)2 with a dimer in the asymmetric unit
(Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., & Sussman,
J.L., 1989, J. Mol. Biol. 206, 787-788). Refinement of the protein structure
(3,148 atoms with Mn and no solvents), with restraints maintaining
noncrystallographic symmetry, converged at an R-factor of 0.207 using all data
from 8.0 to 3.2 A resolution and group thermal parameters. The monomer-monomer
interactions typical of bacterial Fe- and Mn-containing SODs are retained in the
human enzyme, but the dimer-dimer interactions that form the tetramer are very
different from those found in the structure of MnSOD from T. thermophilus. In
human MnSOD one of the dimers is rotated by 84 degrees relative to its
equivalent in the thermophile enzyme. As a result the monomers are arranged in
an approximately tetrahedral array, the dimer-dimer packing is more intimate
than observed in the bacterial MnSOD from T. thermophilus, and the dimers
interdigitate. The metal-ligand interactions, determined by refinement and
verified by computation of omit maps, are identical to those observed in T.
thermophilus MnSOD.
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Figure 4.
Fig. 4. Distances between Ca positions of the human and bacterial
crystals diffracted to -2.8 A resolution, but because they
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Figure 6.
Fig. 6. Electron density in the vicinity
of the Mn binding site of the B chain:
difference (IFo] - IF,I) mapafter X-
PLORrefinement ofamodel from
which the metal ions were omitted (line
4 of Table 1). The positive contoursare
at 40; the peak density at the metal site
is about 60.
\ .
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The above figures are
reprinted
from an Open Access publication published by the Protein Society:
Protein Sci
(1993,
2,
814-825)
copyright 1993.
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Secondary reference #1
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Title
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Characterization of crystals of genetically engineered human manganese superoxide dismutase.
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Authors
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U.G.Wagner,
M.M.Werber,
Y.Beck,
J.R.Hartman,
F.Frolow,
J.L.Sussman.
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Ref.
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J Mol Biol, 1989,
206,
787-788.
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PubMed id
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