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PDBsum entry 1pox
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Oxidoreductase(oxygen as acceptor)
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PDB id
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1pox
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The refined structures of a stabilized mutant and of wild-Type pyruvate oxidase from lactobacillus plantarum.
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Authors
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Y.A.Muller,
G.Schumacher,
R.Rudolph,
G.E.Schulz.
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Ref.
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J Mol Biol, 1994,
237,
315-335.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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The crystal structure of pyruvate oxidase (EC 1.2.3.3) from Lactobacillus
plantarum stabilized by three point mutations has been refined at 2.1 A
resolution using the simulated annealing method. Based on 87,775 independent
reflections in the resolution range 10 to 2.1 A, a final R-factor of 16.2% was
obtained at good model geometry. The wild-type enzyme crystallizes isomorphously
with the stabilized enzyme and has been analyzed at 2.5 A resolution. Pyruvate
oxidase is a homotetramer with point group symmetry D2. One 2-fold axis is
crystallographic, the others are local. The crystallographic asymmetric unit
contains two subunits, and the model consists of the two polypeptide chains
(residues 9 through 593), two FAD, two ThDP*Mg2+ and 739 water molecules. Each
subunit has three domains; the CORE domain, the FAD domain and the ThDP domain.
The FAD-binding chain fold is different from those of other known flavoproteins,
whereas the ThDP-binding chain fold resembles the corresponding folds of the two
other ThDP enzymes whose structure is known, transketolase and pyruvate
decarboxylase. The peptide environment most likely forces the pyrimidine ring of
ThDP into an unusual tautomeric form, which is required for catalysis. The
structural differences between the wild-type and the stabilized enzyme are
small. All three point mutations are at or near to the subunit interfaces,
indicating that they stabilize the quarternary structure as had been deduced
from reconstitution experiments.
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Secondary reference #1
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Title
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Structure of the thiamine- And flavin-Dependent enzyme pyruvate oxidase.
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Authors
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Y.A.Muller,
G.E.Schulz.
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Ref.
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Science, 1993,
259,
965-967.
[DOI no: ]
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PubMed id
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