7B2N
Crystal structure of Chlamydomonas reinhardtii chloroplastic Fructose bisphosphate aldolase
Summary for 7B2N
| Entry DOI | 10.2210/pdb7b2n/pdb |
| Descriptor | Fructose-bisphosphate aldolase 1, chloroplastic, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | fructose bisphosphate aldolase, chlamydomonas reinhardtii, glyceraldehyde-3-phosphate, dihydroxyacetone phosphate, fructose-1, 6-bisphosphate, calvin-benson cycle, photosynthesis |
| Biological source | Chlamydomonas reinhardtii |
| Total number of polymer chains | 8 |
| Total formula weight | 318365.00 |
| Authors | Le Moigne, T.,Lemaire, S.D.,Henri, J. (deposition date: 2020-11-27, release date: 2021-12-08, Last modification date: 2024-05-01) |
| Primary citation | Le Moigne, T.,Sarti, E.,Nourisson, A.,Zaffagnini, M.,Carbone, A.,Lemaire, S.D.,Henri, J. Crystal structure of chloroplast fructose-1,6-bisphosphate aldolase from the green alga Chlamydomonas reinhardtii. J.Struct.Biol., 214:107873-107873, 2022 Cited by PubMed Abstract: The Calvin-Benson cycle fixes carbon dioxide into organic triosephosphates through the collective action of eleven conserved enzymes. Regeneration of ribulose-1,5-bisphosphate, the substrate of Rubisco-mediated carboxylation, requires two lyase reactions catalyzed by fructose-1,6-bisphosphate aldolase (FBA). While cytoplasmic FBA has been extensively studied in non-photosynthetic organisms, functional and structural details are limited for chloroplast FBA encoded by oxygenic phototrophs. Here we determined the crystal structure of plastidial FBA from the unicellular green alga Chlamydomonas reinhardtii (Cr). We confirm that CrFBA folds as a TIM barrel, describe its catalytic pocket and homo-tetrameric state. Multiple sequence profiling classified the photosynthetic paralogs of FBA in a distinct group from non-photosynthetic paralogs. We mapped the sites of thiol- and phospho-based post-translational modifications known from photosynthetic organisms and predict their effects on enzyme catalysis. PubMed: 35680033DOI: 10.1016/j.jsb.2022.107873 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.36 Å) |
Structure validation
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