 |
PDBsum entry 1rgv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
1rgv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Acta Crystallogr D Biol Crystallogr
60:388-391
(2004)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.
|
|
M.Unciuleac,
M.Boll,
E.Warkentin,
U.Ermler.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a central enzyme in the metabolism of
phenolic compounds in anaerobic bacteria. The enzyme catalyzes the reductive
removal of the phenolic hydroxyl group from 4-hydroxybenzoyl-CoA, yielding
benzoyl-CoA and water. 4-HBCR belongs to the xanthine oxidase (XO) family of
molybdenum enzymes which occur as heterodimers, (alphabetagamma)(2). 4-HBCR
clusters and two
FADs. A low-potential Allochromatium vinosum-type ferredoxin containing two
clusters serves as an in vivo electron donor for 4-HBCR. In this work,
the oxygen-sensitive proteins 4-HBCR and the ferredoxin (TaFd) from Thauera
aromatica were crystallized under anaerobic conditions. 4-HBCR crystallized with
PEG 4000 and MPD as precipitant diffracted to about 1.6 A resolution and the
crystals were highly suitable for X-ray structure analysis. Crystals of TaFd
were obtained with (NH(4))(3)PO(4) as precipitant and revealed a solvent content
of 77%, which is remarkably high for a small soluble protein. The structure of
TaFd was solved at 2.9 A resolution by the molecular-replacement method using
the highly related structure of the ferredoxin (CvFd) from A. vinosum as a
cluster can be correlated with their different redox potentials.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
Figure 1.
Figure 1 Reactions catalyzed by benzoyl-CoA reductase (1) and
4-hydroxybenzoyl-CoA reductase (2). In T. aromatica, reduced
ferredoxin serves as in vivo electron donor for both reactions;
it is regenerated by 2-oxoglutarate:ferredoxin oxidoreductase.
|
|
|
|
|
|
| |
The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
388-391)
copyright 2004.
|
|
| |
Figure was
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
M.Heinnickel,
and
J.H.Golbeck
(2007).
Heliobacterial photosynthesis.
|
| |
Photosynth Res,
92,
35-53.
|
|
|
|
|
|
|
P.Giastas,
N.Pinotsis,
G.Efthymiou,
M.Wilmanns,
P.Kyritsis,
J.M.Moulis,
and
I.M.Mavridis
(2006).
The structure of the 2[4Fe-4S] ferredoxin from Pseudomonas aeruginosa at 1.32-A resolution: comparison with other high-resolution structures of ferredoxins and contributing structural features to reduction potential values.
|
| |
J Biol Inorg Chem,
11,
445-458.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
M.Boll,
B.Schink,
A.Messerschmidt,
and
P.M.Kroneck
(2005).
Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism.
|
| |
Biol Chem,
386,
999.
|
|
|
|
|
|
|
M.Unciuleac,
E.Warkentin,
C.C.Page,
M.Boll,
and
U.Ermler
(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.
|
|
|
PDB codes:
|
|
|
|
|
|
|
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.
|
');
}
}
|
Links
