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PDBsum entry 1ryt
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Electron transport
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PDB id
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1ryt
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Contents |
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* Residue conservation analysis
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Nat Struct Biol
3:539-546
(1996)
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PubMed id:
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The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.
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F.deMaré,
D.M.Kurtz,
P.Nordlund.
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ABSTRACT
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We have determined the structure of rubrerythrin, a non-haem iron protein from
the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris
(Hildenborough), by X-ray crystallography. The structure reveals a tetramer of
two-domain subunits. Each subunit contains a four-helix bundle surrounding a
diiron-oxo site and a C-terminal rubredoxin-like FeS4 domain. The diiron-oxo
site contains a larger number of carboxylate ligands and a higher degree of
solvent exposure than do those in other diiron-oxo proteins. The four-helix
bundle of rubrerythrin closely resembles those of the ferritin and
bacterioferritin subunits, suggesting a relationship among these
proteins-consistent with the recently demonstrated ferroxidase activity of
rubrerythrin.
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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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A.F.Pinto,
S.Todorovic,
P.Hildebrandt,
M.Yamazaki,
F.Amano,
S.Igimi,
C.V.Romão,
and
M.Teixeira
(2011).
Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein.
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J Biol Inorg Chem,
16,
501-510.
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Y.Luo,
C.E.Ergenekan,
J.T.Fischer,
M.L.Tan,
and
T.Ichiye
(2010).
The molecular determinants of the increased reduction potential of the rubredoxin domain of rubrerythrin relative to rubredoxin.
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Biophys J,
98,
560-568.
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W.S.Maaty,
B.Wiedenheft,
P.Tarlykov,
N.Schaff,
J.Heinemann,
J.Robison-Cox,
J.Valenzuela,
A.Dougherty,
P.Blum,
C.M.Lawrence,
T.Douglas,
M.J.Young,
and
B.Bothner
(2009).
Something old, something new, something borrowed; how the thermoacidophilic archaeon Sulfolobus solfataricus responds to oxidative stress.
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PLoS One,
4,
e6964.
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A.R.Lambert,
D.Sussman,
B.Shen,
R.Maunus,
J.Nix,
J.Samuelson,
S.Y.Xu,
and
B.L.Stoddard
(2008).
Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding.
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Structure,
16,
558-569.
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PDB codes:
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J.Meyer
(2008).
Iron-sulfur protein folds, iron-sulfur chemistry, and evolution.
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J Biol Inorg Chem,
13,
157-170.
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M.Proudfoot,
S.A.Sanders,
A.Singer,
R.Zhang,
G.Brown,
A.Binkowski,
L.Xu,
J.A.Lukin,
A.G.Murzin,
A.Joachimiak,
C.H.Arrowsmith,
A.M.Edwards,
A.V.Savchenko,
and
A.F.Yakunin
(2008).
Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
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J Mol Biol,
375,
301-315.
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PDB codes:
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A.Hindupur,
D.Liu,
Y.Zhao,
H.D.Bellamy,
M.A.White,
and
R.O.Fox
(2006).
The crystal structure of the E. coli stress protein YciF.
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Protein Sci,
15,
2605-2611.
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PDB code:
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F.Hillmann,
R.J.Fischer,
and
H.Bahl
(2006).
The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a general stress protein.
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Arch Microbiol,
185,
270-276.
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M.H.Sazinsky,
P.W.Dunten,
M.S.McCormick,
A.DiDonato,
and
S.J.Lippard
(2006).
X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase.
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Biochemistry,
45,
15392-15404.
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PDB codes:
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P.Sobrado,
K.S.Lyle,
S.P.Kaul,
M.M.Turco,
I.Arabshahi,
A.Marwah,
and
B.G.Fox
(2006).
Identification of the binding region of the [2Fe-2S] ferredoxin in stearoyl-acyl carrier protein desaturase: insight into the catalytic complex and mechanism of action.
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Biochemistry,
45,
4848-4858.
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I.Friedberg,
and
A.Godzik
(2005).
Connecting the protein structure universe by using sparse recurring fragments.
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Structure,
13,
1213-1224.
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J.B.Vicente,
and
M.Teixeira
(2005).
Redox and spectroscopic properties of the Escherichia coli nitric oxide-detoxifying system involving flavorubredoxin and its NADH-oxidizing redox partner.
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J Biol Chem,
280,
34599-34608.
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J.R.Calhoun,
F.Nastri,
O.Maglio,
V.Pavone,
A.Lombardi,
and
W.F.DeGrado
(2005).
Artificial diiron proteins: from structure to function.
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Biopolymers,
80,
264-278.
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R.B.Iyer,
R.Silaghi-Dumitrescu,
D.M.Kurtz,
and
W.N.Lanzilotta
(2005).
High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins.
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J Biol Inorg Chem,
10,
407-416.
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PDB codes:
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R.E.Stenkamp
(2005).
Anatomy of a trans-cis peptide transition during least-squares refinement of rubrerythrin.
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Acta Crystallogr D Biol Crystallogr,
61,
1599-1602.
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A.May,
F.Hillmann,
O.Riebe,
R.J.Fischer,
and
H.Bahl
(2004).
A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21.
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FEMS Microbiol Lett,
238,
249-254.
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M.V.Weinberg,
F.E.Jenney,
X.Cui,
and
M.W.Adams
(2004).
Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase.
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J Bacteriol,
186,
7888-7895.
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M.Yamasaki,
S.Igimi,
Y.Katayama,
S.Yamamoto,
and
F.Amano
(2004).
Identification of an oxidative stress-sensitive protein from Campylobacter jejuni, homologous to rubredoxin oxidoreductase/rubrerythrin.
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FEMS Microbiol Lett,
235,
57-63.
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W.Tempel,
Z.J.Liu,
F.D.Schubot,
A.Shah,
M.V.Weinberg,
F.E.Jenney,
W.B.Arendall,
M.W.Adams,
J.S.Richardson,
D.C.Richardson,
J.P.Rose,
and
B.C.Wang
(2004).
Structural genomics of Pyrococcus furiosus: X-ray crystallography reveals 3D domain swapping in rubrerythrin.
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Proteins,
57,
878-882.
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PDB code:
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D.T.Logan,
E.Mulliez,
K.M.Larsson,
S.Bodevin,
M.Atta,
P.E.Garnaud,
B.M.Sjoberg,
and
M.Fontecave
(2003).
A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.
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Proc Natl Acad Sci U S A,
100,
3826-3831.
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PDB code:
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M.A.Carrondo
(2003).
Ferritins, iron uptake and storage from the bacterioferritin viewpoint.
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EMBO J,
22,
1959-1968.
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M.Moche,
J.Shanklin,
A.Ghoshal,
and
Y.Lindqvist
(2003).
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates.
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J Biol Chem,
278,
25072-25080.
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PDB codes:
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T.J.Stillman,
P.P.Connolly,
C.L.Latimer,
A.F.Morland,
M.A.Quail,
S.C.Andrews,
A.Treffry,
J.R.Guest,
P.J.Artymiuk,
and
P.M.Harrison
(2003).
Insights into the effects on metal binding of the systematic substitution of five key glutamate ligands in the ferritin of Escherichia coli.
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J Biol Chem,
278,
26275-26286.
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T.Wakagi
(2003).
Sulerythrin, the smallest member of the rubrerythrin family, from a strictly aerobic and thermoacidophilic archaeon, Sulfolobus tokodaii strain 7.
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FEMS Microbiol Lett,
222,
33-37.
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M.Sztukowska,
M.Bugno,
J.Potempa,
J.Travis,
and
D.M.Kurtz
(2002).
Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis.
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Mol Microbiol,
44,
479-488.
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C.M.Gomes,
J.Le Gall,
A.V.Xavier,
and
M.Teixeira
(2001).
Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
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Chembiochem,
2,
583-587.
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H.L.Lumppio,
N.V.Shenvi,
A.O.Summers,
G.Voordouw,
and
D.M.Kurtz
(2001).
Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system.
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J Bacteriol,
183,
101-108.
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A.Lombardi,
C.M.Summa,
S.Geremia,
L.Randaccio,
V.Pavone,
and
W.F.DeGrado
(2000).
Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins.
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Proc Natl Acad Sci U S A,
97,
6298-6305.
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PDB code:
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D.A.Berthold,
M.E.Andersson,
and
P.Nordlund
(2000).
New insight into the structure and function of the alternative oxidase.
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Biochim Biophys Acta,
1460,
241-254.
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B.R.Gibney,
and
P.L.Dutton
(1999).
Histidine placement in de novo-designed heme proteins.
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Protein Sci,
8,
1888-1898.
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C.M.Summa,
A.Lombardi,
M.Lewis,
and
W.F.DeGrado
(1999).
Tertiary templates for the design of diiron proteins.
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Curr Opin Struct Biol,
9,
500-508.
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M.Archer,
A.L.Carvalho,
S.Teixeira,
I.Moura,
J.J.Moura,
F.Rusnak,
and
M.J.Romão
(1999).
Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.
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Protein Sci,
8,
1536-1545.
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PDB codes:
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M.K.Eidsness,
A.E.Burden,
K.A.Richie,
D.M.Kurtz,
R.A.Scott,
E.T.Smith,
T.Ichiye,
B.Beard,
T.Min,
and
C.Kang
(1999).
Modulation of the redox potential of the [Fe(SCys)(4)] site in rubredoxin by the orientation of a peptide dipole.
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Biochemistry,
38,
14803-14809.
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PDB code:
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D.T.Logan,
F.deMaré,
B.O.Persson,
A.Slaby,
B.M.Sjöberg,
and
P.Nordlund
(1998).
Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins.
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Biochemistry,
37,
10798-10807.
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PDB code:
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J.Stubbe,
and
P.Riggs-Gelasco
(1998).
Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase.
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Trends Biochem Sci,
23,
438-443.
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R.A.Grant,
D.J.Filman,
S.E.Finkel,
R.Kolter,
and
J.M.Hogle
(1998).
The crystal structure of Dps, a ferritin homolog that binds and protects DNA.
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Nat Struct Biol,
5,
294-303.
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PDB code:
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H.L.Lumppio,
N.V.Shenvi,
R.P.Garg,
A.O.Summers,
and
D.M.Kurtz
(1997).
A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris (Hildenborough).
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J Bacteriol,
179,
4607-4615.
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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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