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* Residue conservation analysis
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PDB id:
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Oxidoreductase
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Title:
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Structure of adenylylsulfate reductase from the hyperthermophilic archaeoglobus fulgidus at 1.6 resolution
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Structure:
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Adenylylsulfate reductase. Chain: a, c. Fragment: a subunit. Adenylylsulfate reductase. Chain: b, d. Fragment: b subunit. Ec: 1.8.99.2
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Source:
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Archaeoglobus fulgidus dsm 4304. Organism_taxid: 224325. Strain: dsm4304. Strain: dsm4304
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Biol. unit:
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Tetramer (from
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Resolution:
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1.60Å
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R-factor:
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0.180
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R-free:
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0.202
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Authors:
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G.Fritz,A.Roth,A.Schiffer,T.Buechert,G.Bourenkov,H.D.Bartunik, H.Huber,K.O.Stetter,P.M.H.Kroneck,U.Ermler
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Key ref:
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G.Fritz
et al.
(2002).
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
Proc Natl Acad Sci U S A,
99,
1836-1841.
PubMed id:
DOI:
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Date:
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25-Jul-01
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Release date:
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27-Feb-02
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D:
E.C.1.8.99.2
- adenylyl-sulfate reductase.
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Reaction:
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sulfite + A + AMP + 2 H+ = adenosine 5'-phosphosulfate + AH2
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sulfite
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+
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+
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AMP
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+
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2
×
H(+)
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=
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adenosine 5'-phosphosulfate
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+
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AH2
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Cofactor:
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FAD; Fe cation
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FAD
Bound ligand (Het Group name =
FAD)
corresponds exactly
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Fe cation
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
99:1836-1841
(2002)
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PubMed id:
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Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
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G.Fritz,
A.Roth,
A.Schiffer,
T.Büchert,
G.Bourenkov,
H.D.Bartunik,
H.Huber,
K.O.Stetter,
P.M.Kroneck,
U.Ermler.
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ABSTRACT
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The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5'-phosphosulfate, APS)
reductase catalyzes reversibly the reduction of APS to sulfite and AMP. The
structures of APS reductase from the hyperthermophilic Archaeoglobus fulgidus in
the two-electron reduced state and with sulfite bound to FAD are reported at
1.6- and 2.5- resolution, respectively. The FAD-sulfite adduct was detected
after soaking the crystals with APS. This finding and the architecture of the
active site strongly suggest that catalysis involves a nucleophilic attack of
the N5 atom of reduced FAD on the sulfur atom of APS. In view of the high degree
of similarity between APS reductase and fumarate reductase especially with
regard to the FAD-binding alpha-subunit, it is proposed that both subunits
originate from a common ancestor resembling archaeal APS reductase. The two
clusters
from the surface of the protein to FAD. The exceptionally large difference in
reduction potential of these clusters (-60 and -500 mV) can be explained by
interactions of the clusters with the protein matrix.
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Selected figure(s)
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Figure 4.
Fig. 4. The active site channel of APS reductase. Shown
is a cut through the molecular surface of APS reductase to show
the active site channel (blue) and the position of the
cofactors. The active site channel is lined up by a number of
conserved positively charged residues. Almost only the N5 atom
of FAD is accessible to the solvent.
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Figure 5.
Fig. 5. Scheme of the catalytic mechanism of APS
reductase. The mechanism is based on a nucleophilic attack of
the atom N5 of FAD on the sulfate sulfur of APS, thus forming a
FAD-APS intermediate that decays to AMP and a FAD-sulfite
intermediate; the latter was structurally characterized. It is
unclear whether the proton of N5 remains in proximity of the
active site. It might be transferred to the residues Glu-A141 or
Asp-A361.
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Figures were
selected
by an automated process.
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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.Basen,
M.Krüger,
J.Milucka,
J.Kuever,
J.Kahnt,
O.Grundmann,
A.Meyerdierks,
F.Widdel,
and
S.Shima
(2011).
Bacterial enzymes for dissimilatory sulfate reduction in a marine microbial mat (Black Sea) mediating anaerobic oxidation of methane.
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Environ Microbiol,
13,
1370-1379.
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Z.Itzhaki,
E.Akiva,
and
H.Margalit
(2010).
Preferential use of protein domain pairs as interaction mediators: order and transitivity.
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Bioinformatics,
26,
2564-2570.
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Y.L.Chiang,
Y.C.Hsieh,
J.Y.Fang,
E.H.Liu,
Y.C.Huang,
P.Chuankhayan,
J.Jeyakanthan,
M.Y.Liu,
S.I.Chan,
and
C.J.Chen
(2009).
Crystal structure of Adenylylsulfate reductase from Desulfovibrio gigas suggests a potential self-regulation mechanism involving the C terminus of the beta-subunit.
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J Bacteriol,
191,
7597-7608.
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PDB code:
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B.Meyer,
and
J.Kuever
(2008).
Homology Modeling of Dissimilatory APS Reductases (AprBA) of Sulfur-Oxidizing and Sulfate-Reducing Prokaryotes.
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PLoS ONE,
3,
e1514.
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H.Ogata,
A.Goenka Agrawal,
A.P.Kaur,
R.Goddard,
W.Gärtner,
and
W.Lubitz
(2008).
Purification, crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Desulfovibrio vulgaris Miyazaki F.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
1010-1012.
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H.Shibata,
K.Suzuki,
and
S.Kobayashi
(2007).
Menaquinone reduction by an HMT2-like sulfide dehydrogenase from Bacillus stearothermophilus.
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Can J Microbiol,
53,
1091-1100.
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H.Shibata,
and
S.Kobayashi
(2006).
Characterization of a HMT2-like enzyme for sulfide oxidation from Pseudomonas putida.
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Can J Microbiol,
52,
724-730.
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M.Boll,
B.Schink,
A.Messerschmidt,
and
P.M.Kroneck
(2005).
Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism.
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Biol Chem,
386,
999.
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W.Iwasaki,
H.Miyatake,
and
K.Miki
(2005).
Crystal structure of the small form of glucose-inhibited division protein A from Thermus thermophilus HB8.
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Proteins,
61,
1121-1126.
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PDB code:
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A.Messerschmidt,
H.Niessen,
D.Abt,
O.Einsle,
B.Schink,
and
P.M.Kroneck
(2004).
Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.
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Proc Natl Acad Sci U S A,
101,
11571-11576.
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PDB codes:
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M.Soltero-Higgin,
E.E.Carlson,
T.D.Gruber,
and
L.L.Kiessling
(2004).
A unique catalytic mechanism for UDP-galactopyranose mutase.
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Nat Struct Mol Biol,
11,
539-543.
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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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');
}
}
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