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4ZGS

Identification of the pyruvate reductase of Chlamydomonas reinhardtii

Summary for 4ZGS
Entry DOI10.2210/pdb4zgs/pdb
DescriptorPutative D-lactate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
Functional Keywordspyruvate dehydrogenase, fermentation, green alga, biohydrogen, oxidoreductase
Biological sourceChlamydomonas reinhardtii
Total number of polymer chains8
Total formula weight341957.90
Authors
Burgess, S.J.,Hussein, T.,Yeoman, J.A.,Iamshanova, O.,Boehm, M.,Bundy, J.,Bialek, W.,Murray, J.W.,Nixon, P.J. (deposition date: 2015-04-23, release date: 2015-12-02, Last modification date: 2024-01-10)
Primary citationBurgess, S.J.,Taha, H.,Yeoman, J.A.,Iamshanova, O.,Chan, K.X.,Boehm, M.,Behrends, V.,Bundy, J.G.,Bialek, W.,Murray, J.W.,Nixon, P.J.
Identification of the Elusive Pyruvate Reductase of Chlamydomonas reinhardtii Chloroplasts.
Plant Cell.Physiol., 57:82-94, 2016
Cited by
PubMed Abstract: 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.
PubMed: 26574578
DOI: 10.1093/pcp/pcv167
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.461 Å)
Structure validation

237735

数据于2025-06-18公开中

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