7B2N
Crystal structure of Chlamydomonas reinhardtii chloroplastic Fructose bisphosphate aldolase
7B2N の概要
| エントリーDOI | 10.2210/pdb7b2n/pdb |
| 分子名称 | Fructose-bisphosphate aldolase 1, chloroplastic, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| 機能のキーワード | fructose bisphosphate aldolase, chlamydomonas reinhardtii, glyceraldehyde-3-phosphate, dihydroxyacetone phosphate, fructose-1, 6-bisphosphate, calvin-benson cycle, photosynthesis |
| 由来する生物種 | Chlamydomonas reinhardtii |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 318365.00 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.36 Å) |
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