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PDBsum entry 1frd
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Electron transport
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PDB id
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1frd
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Contents |
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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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Molecular structure of the oxidized, recombinant, heterocyst (2fe-2s) ferredoxin from anabaena 7120 determined to 1.7 angstroms resolution
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Structure:
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Heterocyst [2fe-2s] ferredoxin. Chain: a. Engineered: yes
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Source:
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Nostoc sp.. Organism_taxid: 103690. Strain: pcc 7120
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Resolution:
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Authors:
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B.L.Jacobson,Y.K.Chae,J.L.Markley,I.Rayment,H.M.Holden
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Key ref:
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B.L.Jacobson
et al.
(1993).
Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution.
Biochemistry,
32,
6788-6793.
PubMed id:
DOI:
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Date:
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14-Apr-93
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Release date:
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31-May-94
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PROCHECK
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Headers
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References
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P11053
(FERH_NOSS1) -
Ferredoxin, heterocyst from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
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Seq:
Struc:
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99 a.a.
98 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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DOI no:
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Biochemistry
32:6788-6793
(1993)
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PubMed id:
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Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution.
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B.L.Jacobson,
Y.K.Chae,
J.L.Markley,
I.Rayment,
H.M.Holden.
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ABSTRACT
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The [2Fe-2S] ferredoxin produced in the heterocyst cells of Anabaena 7120 plays
a key role in nitrogen fixation, where it serves as an electron acceptor from
various sources and an electron donor to nitrogenase. The three-dimensional
structure of this ferredoxin has now been determined and refined to a
crystallographic R value of 16.7%, with all measured X-ray data from 30.0 to 1.7
A. The molecular motif of this ferredoxin is similar to that of other plant-type
ferredoxins with the iron-sulfur cluster located toward the outer edge of the
molecule and the irons tetrahedrally coordinated by both inorganic sulfurs and
sulfurs provided by protein cysteinyl residues. The overall secondary structure
of the molecule consists of seven strands of beta-pleated sheet, two
alpha-helices, and seven type I turns. It is of special interest that 4 of the
22 amino acid positions thought to be absolutely conserved in nonhalophilic
ferredoxins are different in the heterocyst form of the protein. Three of these
positions are located in the metal-cluster binding loop.
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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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M.Vidakovic,
C.R.Crossnoe,
C.Neidre,
K.Kim,
K.L.Krause,
and
J.P.Germanas
(2003).
Reactivity of reduced [2Fe-2S] ferredoxins parallels host susceptibility to nitroimidazoles.
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Antimicrob Agents Chemother,
47,
302-308.
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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.Armengaud,
G.Sainz,
Y.Jouanneau,
and
L.C.Sieker
(2001).
Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus.
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Acta Crystallogr D Biol Crystallogr,
57,
301-303.
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PDB code:
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A.V.Grinberg,
F.Hannemann,
B.Schiffler,
J.Müller,
U.Heinemann,
and
R.Bernhardt
(2000).
Adrenodoxin: structure, stability, and electron transfer properties.
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Proteins,
40,
590-612.
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S.Dai,
C.Schwendtmayer,
P.Schürmann,
S.Ramaswamy,
and
H.Eklund
(2000).
Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.
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Science,
287,
655-658.
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PDB code:
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B.B.Singh,
I.Curdt,
C.Jakobs,
D.Schomburg,
P.S.Bisen,
and
H.Böhme
(1999).
Identification of amino acids responsible for the oxygen sensitivity of ferredoxins from Anabaena variabilis using site-directed mutagenesis.
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Biochim Biophys Acta,
1412,
288-294.
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M.T.Bes,
E.Parisini,
L.A.Inda,
L.M.Saraiva,
M.L.Peleato,
and
G.M.Sheldrick
(1999).
Crystal structure determination at 1.4 A resolution of ferredoxin from the green alga Chlorella fusca.
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Structure,
7,
1201-1211.
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PDB code:
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R.Morales,
M.H.Charon,
G.Hudry-Clergeon,
Y.Pétillot,
S.Norager,
M.Medina,
and
M.Frey
(1999).
Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes.
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Biochemistry,
38,
15764-15773.
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PDB codes:
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T.Akashi,
T.Matsumura,
T.Ideguchi,
K.Iwakiri,
T.Kawakatsu,
I.Taniguchi,
and
T.Hase
(1999).
Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase.
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J Biol Chem,
274,
29399-29405.
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Y.S.Jung,
H.S.Gao-Sheridan,
J.Christiansen,
D.R.Dean,
and
B.K.Burgess
(1999).
Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein.
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J Biol Chem,
274,
32402-32410.
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A.Müller,
J.J.Müller,
Y.A.Muller,
H.Uhlmann,
R.Bernhardt,
and
U.Heinemann
(1998).
New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108).
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Structure,
6,
269-280.
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PDB code:
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B.Xia,
B.F.Volkman,
and
J.L.Markley
(1998).
Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.
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Biochemistry,
37,
3965-3973.
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C.Binda,
A.Coda,
A.Aliverti,
G.Zanetti,
and
A.Mattevi
(1998).
Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution.
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Acta Crystallogr D Biol Crystallogr,
54,
1353-1358.
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PDB code:
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J.K.Hurley,
A.M.Weber-Main,
M.T.Stankovich,
M.M.Benning,
J.B.Thoden,
J.L.Vanhooke,
H.M.Holden,
Y.K.Chae,
B.Xia,
H.Cheng,
J.L.Markley,
M.Martinez-Júlvez,
C.Gómez-Moreno,
J.L.Schmeits,
and
G.Tollin
(1997).
Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants.
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Biochemistry,
36,
11100-11117.
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PDB codes:
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L.Huang,
X.Weng,
F.Hofer,
G.S.Martin,
and
S.H.Kim
(1997).
Three-dimensional structure of the Ras-interacting domain of RalGDS.
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Nat Struct Biol,
4,
609-615.
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PDB code:
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F.Frolow,
M.Harel,
J.L.Sussman,
M.Mevarech,
and
M.Shoham
(1996).
Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin.
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Nat Struct Biol,
3,
452-458.
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PDB code:
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H.Nishida,
and
K.Miki
(1996).
Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner.
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Proteins,
26,
32-41.
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M.S.Vidakovic,
G.Fraczkiewicz,
and
J.P.Germanas
(1996).
Expression and spectroscopic characterization of the hydrogenosomal [2Fe-2S] ferredoxin from the protozoan Trichomonas vaginalis.
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J Biol Chem,
271,
14734-14739.
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M.Vidakovic,
and
J.P.Germanas
(1996).
Electrostatic effects in electron transfer reactions of [2Fe-2S] ferredoxins with inorganic reagents.
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Protein Sci,
5,
1793-1799.
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S.Schmitz,
F.Navarro,
C.K.Kutzki,
F.J.Florencio,
and
H.Böhme
(1996).
Glutamate 94 of [2Fe-2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803.
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Biochim Biophys Acta,
1277,
135-140.
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H.Uhlmann,
and
R.Bernhardt
(1995).
The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function.
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J Biol Chem,
270,
29959-29966.
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J.K.Hurley,
M.S.Caffrey,
J.L.Markley,
H.Cheng,
B.Xia,
Y.K.Chae,
H.M.Holden,
and
G.Tollin
(1995).
Mutations of surface residues in Anabaena vegetative and heterocyst ferredoxin that affect thermodynamic stability as determined by guanidine hydrochloride denaturation.
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Protein Sci,
4,
58-64.
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B.Schrautemeier,
A.Cassing,
and
H.Böhme
(1994).
Characterization of the genome region encoding an fdxH-type ferredoxin and a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing cyanobacterium Plectonema boryanum PCC 73110.
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J Bacteriol,
176,
1037-1046.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
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Links
