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PDBsum entry 1sb3
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Oxidoreductase
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PDB id
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1sb3
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Contents |
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761 a.a.
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323 a.a.
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161 a.a.
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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 4-hydroxybenzoyl-coa reductase from thauera aromatica
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Structure:
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4-hydroxybenzoyl-coa reductase alpha subunit. Chain: a, d. 4-hydroxybenzoyl-coa reductase beta subunit. Chain: b, e. 4-hydroxybenzoyl-coa reductase gamma subunit. Chain: c, f. Ec: 1.3.99.20
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Source:
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Thauera aromatica. Organism_taxid: 59405. Strain: strain k, dsmz 6984. Strain: strain k, dsmz 6984
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Biol. unit:
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Hexamer (from
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Resolution:
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2.20Å
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R-factor:
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0.171
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R-free:
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0.205
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Authors:
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M.Unciuleac,E.Warkentin,C.C.Page,M.Boll,U.Ermler
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Key ref:
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M.Unciuleac
et al.
(2004).
Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow.
Structure,
12,
2249-2256.
PubMed id:
DOI:
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Date:
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10-Feb-04
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Release date:
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21-Dec-04
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PROCHECK
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Headers
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References
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O33819
(HCRA_THAAR) -
4-hydroxybenzoyl-CoA reductase subunit alpha from Thauera aromatica
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Seq:
Struc:
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769 a.a.
761 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.1.1.7.1
- 4-hydroxybenzoyl-CoA reductase.
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Reaction:
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oxidized 2[4Fe-4S]-[ferredoxin] + benzoyl-CoA + H2O = 4-hydroxybenzoyl- CoA + reduced 2[4Fe-4S]-[ferredoxin] + 2 H+
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oxidized 2[4Fe-4S]-[ferredoxin]
Bound ligand (Het Group name = )
matches with 43.42% similarity
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+
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benzoyl-CoA
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+
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H2O
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=
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4-hydroxybenzoyl- CoA
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+
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reduced 2[4Fe-4S]-[ferredoxin]
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+
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2
×
H(+)
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Cofactor:
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Flavin; Iron-sulfur; Mo cation
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Flavin
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Iron-sulfur
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Mo 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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Structure
12:2249-2256
(2004)
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PubMed id:
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Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow.
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M.Unciuleac,
E.Warkentin,
C.C.Page,
M.Boll,
U.Ermler.
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ABSTRACT
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The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA
reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic
degradation of phenolic compounds and belongs to the xanthine oxidase (XO)
family of molybdenum enzymes. Its X-ray structure was established at 1.6 A
resolution. The most pronounced difference between 4-HBCR and other structurally
characterized members of the XO family is the insertion of 40 amino acids within
cluster at a distance of
16.5 A to the isoalloxazine ring of FAD. The architecture of 4-HBCR and
concomitantly performed electron transfer rate calculations suggest an inverted
cluster to
the Mo over a distance of 55 A. The binding site of 4-hydroxybenzoyl-CoA is
located in an 18 A long channel lined up by several aromatic side chains around
the aromatic moiety, which are proposed to shield and stabilize the postulated
radical intermediates during catalysis.
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Selected figure(s)
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Figure 1.
Figure 1. Reaction Catalyzed by 4-Hydroxybenzoyl-CoA
Reductase
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
2249-2256)
copyright 2004.
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Figure was
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.Neumann,
and
S.Leimkühler
(2011).
The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria.
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Biochem Res Int,
2011,
850924.
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M.Carmona,
M.T.Zamarro,
B.Blázquez,
G.Durante-Rodríguez,
J.F.Juárez,
J.A.Valderrama,
M.J.Barragán,
J.L.García,
and
E.Díaz
(2009).
Anaerobic catabolism of aromatic compounds: a genetic and genomic view.
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Microbiol Mol Biol Rev,
73,
71.
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M.J.Romão
(2009).
Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview.
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Dalton Trans,
(),
4053-4068.
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G.Fuchs
(2008).
Anaerobic metabolism of aromatic compounds.
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Ann N Y Acad Sci,
1125,
82-99.
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J.Johannes,
A.Bluschke,
N.Jehmlich,
M.von Bergen,
and
M.Boll
(2008).
Purification and characterization of active-site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens.
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J Bacteriol,
190,
6493-6500.
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F.Peters,
D.Heintz,
J.Johannes,
A.van Dorsselaer,
and
M.Boll
(2007).
Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens.
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J Bacteriol,
189,
4729-4738.
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C.D.Brondino,
M.J.Romão,
I.Moura,
and
J.J.Moura
(2006).
Molybdenum and tungsten enzymes: the xanthine oxidase family.
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Curr Opin Chem Biol,
10,
109-114.
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W.Buckel,
and
B.T.Golding
(2006).
Radical enzymes in anaerobes.
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Annu Rev Microbiol,
60,
27-49.
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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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M.Boll,
and
G.Fuchs
(2005).
Unusual reactions involved in anaerobic metabolism of phenolic compounds.
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Biol Chem,
386,
989-997.
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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.
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Links
