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PDBsum entry 1rof
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Electron transport
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PDB id
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1rof
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Contents |
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* Residue conservation analysis
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Eur J Biochem
237:726-735
(1996)
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PubMed id:
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An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4-S4] ferredoxin.
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H.Sticht,
G.Wildegger,
D.Bentrop,
B.Darimont,
R.Sterner,
P.Rösch.
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ABSTRACT
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The solution structure of the 60-residue 1[Fe4-S4] ferredoxin from the
hyperthermophilic bacterium Thermotoga maritima was determined based on 683
distance and 35 dihedral angle restraints that were obtained from NMR data. In
addition, data known from crystallographic studies of ferredoxins was used for
modeling of the iron-sulfur cluster and its environment. The protein shows a
globular fold very similar to the fold of the related 1[Fe4-S4] ferredoxins from
Desulfovibrio gigas and Desulfovibrio africanus, and elements of regular
secondary structure similar to those in other ferredoxins were found in the T.
maritima protein. In particular, the T. maritima protein displayed a beta-sheet
structure made up of strands located at the very NH(2) and COOH termini of the
protein, and an internal alpha-helix. The internal beta-sheet observed in the D.
gigas and D. africanus ferredoxins could not be confirmed in T. maritima
ferredoxin and is thus suggested to be only weakly present or even absent in
this protein. This result suggests that thermostability in ferredoxins is not
necessarily correlated with the content of stable elements of regular secondary
structure.
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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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P.Giastas,
N.Pinotsis,
G.Efthymiou,
M.Wilmanns,
P.Kyritsis,
J.M.Moulis,
and
I.M.Mavridis
(2006).
The structure of the 2[4Fe-4S] ferredoxin from Pseudomonas aeruginosa at 1.32-A resolution: comparison with other high-resolution structures of ferredoxins and contributing structural features to reduction potential values.
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J Biol Inorg Chem,
11,
445-458.
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PDB code:
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B.W.Beck,
Q.Xie,
and
T.Ichiye
(2001).
Sequence determination of reduction potentials by cysteinyl hydrogen bonds and peptide pipoles in [4Fe-4S] ferredoxins.
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Biophys J,
81,
601-613.
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P.L.Wang,
L.Calzolai,
K.L.Bren,
Q.Teng,
F.E.Jenney,
P.S.Brereton,
J.B.Howard,
M.W.Adams,
and
G.N.La Mar
(1999).
Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity.
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Biochemistry,
38,
8167-8178.
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C.Liang,
and
K.Mislow
(1997).
Topological chirality of iron-sulfur proteins.
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Biopolymers,
42,
411-414.
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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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Links
