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PDBsum entry 1s3a
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Oxidoreductase
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PDB id
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1s3a
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References listed in PDB file
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Key reference
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Title
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The oxidized subunit b8 from human complex i adopts a thioredoxin fold.
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Authors
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C.Brockmann,
A.Diehl,
K.Rehbein,
H.Strauss,
P.Schmieder,
B.Korn,
R.Kühne,
H.Oschkinat.
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Ref.
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Structure, 2004,
12,
1645-1654.
[DOI no: ]
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PubMed id
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Abstract
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Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several
nuclear-encoded supernumerary subunits that are not present in bacterial complex
I. Its solution structure shows a thioredoxin fold with highest similarities to
the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp.
Interestingly, these proteins contain active sites in the same area, where the
disulfide bond of oxidized CI-B8 is located. The redox potential of this
disulfide bond is -251.6 mV, comparing well to that of disulfides in other
thioredoxin-like proteins. Analysis of the structure reveals a surface area that
is exclusively composed of highly conserved residues and thus most likely a
subunit interaction site within complex I.
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Figure 3.
Figure 3. Relaxation Rate Measurements and Amount of
Interresidue NOEs per Residue(A) This panel shows the
distribution of NOE-based interresidue restraints on the
sequence of CI-B8.(B) This panel shows the 15N-T1/T[2] ratios
for each amino acid.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
1645-1654)
copyright 2004.
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