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PDBsum entry 1sp8
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Oxidoreductase
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PDB id
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1sp8
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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4-hydroxyphenylpyruvate dioxygenase
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Structure:
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4-hydroxyphenylpyruvate dioxygenase. Chain: a, b, c, d. Engineered: yes
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Source:
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Zea mays. Organism_taxid: 4577. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Dimer (from
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Resolution:
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2.00Å
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R-factor:
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0.275
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R-free:
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0.324
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Authors:
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I.M.Fritze,L.Linden,J.Freigang,G.Auerbach,R.Huber,S.Steinbacher
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Key ref:
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I.M.Fritze
et al.
(2004).
The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.
Plant Physiol,
134,
1388-1400.
PubMed id:
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Date:
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16-Mar-04
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Release date:
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21-Sep-04
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Key: |
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Secondary structure |
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CATH domain |
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Plant Physiol
134:1388-1400
(2004)
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PubMed id:
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The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.
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I.M.Fritze,
L.Linden,
J.Freigang,
G.Auerbach,
R.Huber,
S.Steinbacher.
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ABSTRACT
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The transformation of 4-hydroxyphenylpyruvate to homogentisate, catalyzed by
4-hydroxyphenylpyruvate dioxygenase (HPPD), plays an important role in degrading
aromatic amino acids. As the reaction product homogentisate serves as aromatic
precursor for prenylquinone synthesis in plants, the enzyme is an interesting
target for herbicides. In this study we report the first x-ray structures of the
plant HPPDs of Zea mays and Arabidopsis in their substrate-free form at 2.0 A
and 3.0 A resolution, respectively. Previous biochemical characterizations have
demonstrated that eukaryotic enzymes behave as homodimers in contrast to
prokaryotic HPPDs, which are homotetramers. Plant and bacterial enzymes share
the overall fold but use orthogonal surfaces for oligomerization. In addition,
comparison of both structures provides direct evidence that the C-terminal helix
gates substrate access to the active site around a nonheme ferrous iron center.
In the Z. mays HPPD structure this helix packs into the active site,
sequestering it completely from the solvent. In contrast, in the Arabidopsis
structure this helix tilted by about 60 degrees into the solvent and leaves the
active site fully accessible. By elucidating the structure of plant HPPD enzymes
we aim to provide a structural basis for the development of new herbicides.
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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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W.Ren,
L.Zhao,
L.Zhang,
Y.Wang,
L.Cui,
Y.Tang,
X.Sun,
and
K.Tang
(2011).
Molecular cloning and characterization of 4-hydroxyphenylpyruvate dioxygenase gene from Lactuca sativa.
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J Plant Physiol,
168,
1076-1083.
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C.W.Riggins,
Y.Peng,
C.N.Stewart,
and
P.J.Tranel
(2010).
Characterization of de novo transcriptome for waterhemp (Amaranthus tuberculatus) using GS-FLX 454 pyrosequencing and its application for studies of herbicide target-site genes.
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Pest Manag Sci,
66,
1042-1052.
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P.He,
and
G.R.Moran
(2009).
We two alone will sing: the two-substrate alpha-keto acid-dependent oxygenases.
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Curr Opin Chem Biol,
13,
443-450.
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K.E.Keith,
L.Killip,
P.He,
G.R.Moran,
and
M.A.Valvano
(2007).
Burkholderia cenocepacia C5424 produces a pigment with antioxidant properties using a homogentisate intermediate.
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J Bacteriol,
189,
9057-9065.
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S.Loprasert,
W.Whangsuk,
J.M.Dubbs,
R.Sallabhan,
K.Somsongkul,
and
S.Mongkolsuk
(2007).
HpdR is a transcriptional activator of Sinorhizobium meliloti hpdA, which encodes a herbicide-targeted 4-hydroxyphenylpyruvate dioxygenase.
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J Bacteriol,
189,
3660-3664.
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S.S.Yoon,
A.C.Karabulut,
J.D.Lipscomb,
R.F.Hennigan,
S.V.Lymar,
S.L.Groce,
A.B.Herr,
M.L.Howell,
P.J.Kiley,
M.J.Schurr,
B.Gaston,
K.H.Choi,
H.P.Schweizer,
and
D.J.Hassett
(2007).
Two-pronged survival strategy for the major cystic fibrosis pathogen, Pseudomonas aeruginosa, lacking the capacity to degrade nitric oxide during anaerobic respiration.
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EMBO J,
26,
3662-3672.
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V.Purpero,
and
G.R.Moran
(2007).
The diverse and pervasive chemistries of the alpha-keto acid dependent enzymes.
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J Biol Inorg Chem,
12,
587-601.
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M.L.Neidig,
A.Decker,
O.W.Choroba,
F.Huang,
M.Kavana,
G.R.Moran,
J.B.Spencer,
and
E.I.Solomon
(2006).
Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes.
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Proc Natl Acad Sci U S A,
103,
12966-12973.
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X.Li,
M.Guo,
J.Fan,
W.Tang,
D.Wang,
H.Ge,
H.Rong,
M.Teng,
L.Niu,
Q.Liu,
and
Q.Hao
(2006).
Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases.
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Protein Sci,
15,
761-773.
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C.Schneider
(2005).
Chemistry and biology of vitamin E.
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Mol Nutr Food Res,
49,
7.
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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
