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PDBsum entry 1dox
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Electron transport
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PDB id
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1dox
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* Residue conservation analysis
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PDB id:
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Electron transport
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Title:
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1h and 15n sequential assignment, secondary structure and tertiary fold of [2fe-2s] ferredoxin from synechocystis sp. Pcc 6803
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Structure:
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Ferredoxin [2fe-2s]. Chain: a. Other_details: plant type ferredoxin, no disulfide bond
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Source:
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Synechocystis sp.. Organism_taxid: 1148. Strain: pcc 6803
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NMR struc:
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3 models
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Authors:
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C.Lelong,P.Setif,H.Bottin,F.Andre,J.M.Neumann
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Key ref:
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C.Lelong
et al.
(1995).
1H and 15N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803.
Biochemistry,
34,
14462-14473.
PubMed id:
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Date:
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14-Sep-95
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Release date:
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08-Mar-96
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PROCHECK
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Headers
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References
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P27320
(FER_SYNY3) -
Ferredoxin-1 from Synechocystis sp. (strain PCC 6803 / Kazusa)
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Seq:
Struc:
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97 a.a.
96 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Biochemistry
34:14462-14473
(1995)
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PubMed id:
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1H and 15N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803.
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C.Lelong,
P.Sétif,
H.Bottin,
F.André,
J.M.Neumann.
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ABSTRACT
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The [2Fe-2S] ferredoxin extracted from Synechocystis sp. PCC 6803 was studied by
1H and 15N nuclear magnetic resonance. Sequence-specific 1H and 15N assignment
of amino acid residues far from the paramagnetic cluster (distance higher than 8
A) was performed. Interresidue NOE constraints have allowed the identification
of several secondary structure elements: one beta sheet composed of four beta
strands, one alpha helix, and two alpha helix turns. The analysis of
interresidue NOEs suggests the existence of a disulfide bridge between the
cysteine residues 18 and 85. Such a disulfide bridge has never been observed in
plant-type ferredoxins. Structure modeling using the X-PLOR program was
performed with or without assuming the existence of a disulfide bridge. As a
result, two structure families were obtained with rms deviations of 2.2 A. Due
to the lack of NOE connectivities resulting from the paramagnetic effect from
the [2Fe-2S] cluster, the structures were not well resolved in the region
surrounding the [2Fe-2S] cluster, at both extremities of the alpha helix and the
C and N terminus segments. In contrast, when taken separately, the beta sheet
and the alpha helix were well defined. This work is the first report of a
structure model of a plant-type [2Fe-2S] Fd in solution.
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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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S.Dai,
R.Friemann,
D.A.Glauser,
F.Bourquin,
W.Manieri,
P.Schürmann,
and
H.Eklund
(2007).
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase.
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Nature,
448,
92-96.
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PDB codes:
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M.E.Boyer,
C.W.Wang,
and
J.R.Swartz
(2006).
Simultaneous expression and maturation of the iron-sulfur protein ferredoxin in a cell-free system.
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Biotechnol Bioeng,
94,
128-138.
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M.Nouailler,
X.Morelli,
O.Bornet,
B.Chetrit,
Z.Dermoun,
and
F.Guerlesquin
(2006).
Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex.
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Protein Sci,
15,
1369-1378.
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PDB code:
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I.Bertini,
C.Luchinat,
A.Provenzani,
A.Rosato,
and
P.R.Vasos
(2002).
Browsing gene banks for Fe2S2 ferredoxins and structural modeling of 88 plant-type sequences: an analysis of fold and function.
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Proteins,
46,
110-127.
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J.Meyer,
M.D.Clay,
M.K.Johnson,
A.Stubna,
E.Münck,
C.Higgins,
and
P.Wittung-Stafshede
(2002).
A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond.
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Biochemistry,
41,
3096-3108.
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P.Barth,
I.Guillouard,
P.Sétif,
and
B.Lagoutte
(2000).
Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin.
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J Biol Chem,
275,
7030-7036.
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R.Kümmerle,
M.Atta,
J.Scuiller,
J.Gaillard,
and
J.Meyer
(1999).
Structural similarities between the N-terminal domain of Clostridium pasteurianum hydrogenase and plant-type ferredoxins.
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Biochemistry,
38,
1938-1943.
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T.C.Pochapsky,
N.U.Jain,
M.Kuti,
T.A.Lyons,
and
J.Heymont
(1999).
A refined model for the solution structure of oxidized putidaredoxin.
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Biochemistry,
38,
4681-4690.
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PDB code:
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M.Poncelet,
C.Cassier-Chauvat,
X.Leschelle,
H.Bottin,
and
F.Chauvat
(1998).
Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC6803 by plasmid shuffling.
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Mol Microbiol,
28,
813-821.
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P.Barth,
B.Lagoutte,
and
P.Sétif
(1998).
Ferredoxin reduction by photosystem I from Synechocystis sp. PCC 6803: toward an understanding of the respective roles of subunits PsaD and PsaE in ferredoxin binding.
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Biochemistry,
37,
16233-16241.
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B.Baumann,
H.Sticht,
M.Schärpf,
M.Sutter,
W.Haehnel,
and
P.Rösch
(1996).
Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.
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Biochemistry,
35,
12831-12841.
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PDB code:
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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
codes are
shown on the right.
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