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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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The 2 angstrom structure of 6-oxo camphor hydrolase: new structural diversity in the crotonase superfamily
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Structure:
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6-oxo camphor hydrolase. Chain: a, b, c, d, e, f. Synonym: camk. Engineered: yes
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Source:
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Rhodococcus erythropolis. Actinomycete. Organism_taxid: 1833. Strain: ncimb 9784. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Biol. unit:
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Hexamer (from PDB file)
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Resolution:
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2.00Å
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R-factor:
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0.149
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R-free:
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0.190
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Authors:
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G.Grogan,J.L.Whittingham,J.P.Turkenburg,C.S.Verma,M.A.Walsh
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Key ref:
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J.L.Whittingham
et al.
(2003).
The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.
J Biol Chem,
278,
1744-1750.
PubMed id:
DOI:
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Date:
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04-Dec-02
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Release date:
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24-Jan-03
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PROCHECK
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Headers
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References
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Q93TU6
(Q93TU6_9NOCA) -
6-oxocamphor hydrolase
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Seq:
Struc:
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257 a.a.
249 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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1 term
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Biochemical function
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catalytic activity
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2 terms
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DOI no:
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J Biol Chem
278:1744-1750
(2003)
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PubMed id:
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The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.
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J.L.Whittingham,
J.P.Turkenburg,
C.S.Verma,
M.A.Walsh,
G.Grogan.
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ABSTRACT
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6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily that
catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a
retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N.
J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572). The native
structure of OCH has been solved at 2.0-A resolution with selenomethionine
multiple wave anomalous dispersion and refined to a final R(free) of 19.0. The
structure of OCH consists of a dimer of trimers that resembles the
"parent" enzyme of the superfamily, enoyl-CoA hydratase. In contrast
to enoyl-CoA hydratase, however, two octahedrally coordinated sodium atoms are
found at the 3-fold axis of the hexamer of OCH, and the C-terminal helix of OCH
does not form a discrete domain. Models of the substrate, 6-oxo camphor, and a
proposed enolate intermediate in the putative active site suggest possible
mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.
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Selected figure(s)
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Figure 3.
Fig. 3. Reactions catalyzed by representative members of
the crotonase superfamily.
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Figure 4.
Fig. 4. Ribbon diagrams showing two views of the OCH
hexamer: perpendicular to (a) and parallel to (b) the hexamer
3-fold axis. For clarity, each monomer of the trimer is colored
differently, and the sodium ions are shown as yellow spheres.
The figure was made using BOBSCRIPT (29).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
1744-1750)
copyright 2003.
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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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J.Bains,
R.Leon,
and
M.J.Boulanger
(2009).
Structural and biophysical characterization of BoxC from Burkholderia xenovorans LB400: a novel ring-cleaving enzyme in the crotonase superfamily.
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J Biol Chem, 284,
16377-16385.
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PDB code:
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K.Kurimoto,
K.Kuwasako,
A.M.Sandercock,
S.Unzai,
C.V.Robinson,
Y.Muto,
and
S.Yokoyama
(2009).
AU-rich RNA-binding induces changes in the quaternary structure of AUH.
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Proteins, 75,
360-372.
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PDB codes:
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P.M.Leonard,
A.M.Brzozowski,
A.Lebedev,
C.M.Marshall,
D.J.Smith,
C.S.Verma,
N.J.Walton,
and
G.Grogan
(2006).
The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin.
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Acta Crystallogr D Biol Crystallogr, 62,
1494-1501.
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PDB code:
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J.M.Johnston,
V.L.Arcus,
and
E.N.Baker
(2005).
Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms.
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Acta Crystallogr D Biol Crystallogr, 61,
1199-1206.
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P.A.Hubbard,
W.Yu,
H.Schulz,
and
J.J.Kim
(2005).
Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial Delta3, Delta2-enoyl-CoA isomerase.
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Protein Sci, 14,
1545-1555.
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PDB code:
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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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Links
