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PDBsum entry 4zgs
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Oxidoreductase
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PDB id
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4zgs
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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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Identification of the pyruvate reductase of chlamydomonas reinhardtii
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Structure:
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Putative d-lactate dehydrogenase. Chain: a, b, c, d, e, f, g, h. Fragment: unp residues 45-421. Synonym: pyruvate reductase. Engineered: yes
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Source:
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Chlamydomonas reinhardtii. Organism_taxid: 3055. Organelle: chloroplast. Gene: cre07.G324550. Expressed in: escherichia coli krx. Expression_system_taxid: 1452720.
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Resolution:
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2.46Å
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R-factor:
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0.205
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R-free:
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0.254
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Authors:
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S.J.Burgess,T.Hussein,J.A.Yeoman,O.Iamshanova,M.Boehm,J.Bundy, W.Bialek,J.W.Murray,P.J.Nixon
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Key ref:
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S.J.Burgess
et al.
(2016).
Identification of the Elusive Pyruvate Reductase of Chlamydomonas reinhardtii Chloroplasts.
Plant Cell Physiol,
57,
82-94.
PubMed id:
DOI:
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Date:
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23-Apr-15
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Release date:
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02-Dec-15
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PROCHECK
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Headers
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References
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B0LUZ5
(B0LUZ5_CHLRE) -
Putative D-lactate dehydrogenase from Chlamydomonas reinhardtii
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Seq:
Struc:
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421 a.a.
346 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Plant Cell Physiol
57:82-94
(2016)
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PubMed id:
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Identification of the Elusive Pyruvate Reductase of Chlamydomonas reinhardtii Chloroplasts.
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S.J.Burgess,
H.Taha,
J.A.Yeoman,
O.Iamshanova,
K.X.Chan,
M.Boehm,
V.Behrends,
J.G.Bundy,
W.Bialek,
J.W.Murray,
P.J.Nixon.
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ABSTRACT
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Under anoxic conditions the green alga Chlamydomonas reinhardtii activates
various fermentation pathways leading to the creation of formate, acetate,
ethanol and small amounts of other metabolites including d-lactate and hydrogen.
Progress has been made in identifying the enzymes involved in these pathways and
their subcellular locations; however, the identity of the enzyme involved in
reducing pyruvate to d-lactate has remained unclear. Based on sequence
comparisons, enzyme activity measurements, X-ray crystallography, biochemical
fractionation and analysis of knock-down mutants, we conclude that pyruvate
reduction in the chloroplast is catalyzed by a tetrameric NAD(+)-dependent
d-lactate dehydrogenase encoded by Cre07.g324550. Its expression during aerobic
growth supports a possible function as a 'lactate valve' for the export of
lactate to the mitochondrion for oxidation by cytochrome-dependent d-lactate
dehydrogenases and by glycolate dehydrogenase. We also present a revised spatial
model of fermentation based on our immunochemical detection of the likely
pyruvate decarboxylase, PDC3, in the cytoplasm.
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