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| | ==Identification of the pyruvate reductase of Chlamydomonas reinhardtii== | | ==Identification of the pyruvate reductase of Chlamydomonas reinhardtii== |
| - | <StructureSection load='4zgs' size='340' side='right' caption='[[4zgs]], [[Resolution|resolution]] 2.46Å' scene=''> | + | <StructureSection load='4zgs' size='340' side='right'caption='[[4zgs]], [[Resolution|resolution]] 2.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zgs]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZGS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zgs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZGS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cre07.g324550 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgs OCA], [https://pdbe.org/4zgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zgs RCSB], [https://www.ebi.ac.uk/pdbsum/4zgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgs ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lactate_dehydrogenase D-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.28 1.1.1.28] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgs OCA], [http://pdbe.org/4zgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zgs RCSB], [http://www.ebi.ac.uk/pdbsum/4zgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B0LUZ5_CHLRE B0LUZ5_CHLRE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| - | [[Category: D-lactate dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bialek, W]] | + | [[Category: Bialek W]] |
| - | [[Category: Boehm, M]] | + | [[Category: Boehm M]] |
| - | [[Category: Bundy, J]] | + | [[Category: Bundy J]] |
| - | [[Category: Burgess, S J]] | + | [[Category: Burgess SJ]] |
| - | [[Category: Hussein, T]] | + | [[Category: Hussein T]] |
| - | [[Category: Iamshanova, O]] | + | [[Category: Iamshanova O]] |
| - | [[Category: Murray, J W]] | + | [[Category: Murray JW]] |
| - | [[Category: Nixon, P J]] | + | [[Category: Nixon PJ]] |
| - | [[Category: Yeoman, J A]] | + | [[Category: Yeoman JA]] |
| - | [[Category: Biohydrogen]]
| + | |
| - | [[Category: Fermentation]]
| + | |
| - | [[Category: Green alga]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pyruvate dehydrogenase]]
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| Structural highlights
Function
B0LUZ5_CHLRE
Publication Abstract from PubMed
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 sub-cellular 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 catalysed 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.
Identification Of The Elusive Pyruvate Reductase Of Chlamydomonas reinhardtii Chloroplasts.,Burgess SJ, Taha H, Yeoman JA, Iamshanova O, Chan KX, Boehm M, Bundy J, Bialek W, Murray JW, Nixon PJ Plant Cell Physiol. 2015 Nov 15. pii: pcv167. PMID:26574578[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burgess SJ, Taha H, Yeoman JA, Iamshanova O, Chan KX, Boehm M, Bundy J, Bialek W, Murray JW, Nixon PJ. Identification Of The Elusive Pyruvate Reductase Of Chlamydomonas reinhardtii Chloroplasts. Plant Cell Physiol. 2015 Nov 15. pii: pcv167. PMID:26574578 doi:http://dx.doi.org/10.1093/pcp/pcv167
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