دورية أكاديمية
Crystal structure of chloroplast fructose-1,6-bisphosphate aldolase from the green alga Chlamydomonas reinhardtii
| العنوان: | Crystal structure of chloroplast fructose-1,6-bisphosphate aldolase from the green alga Chlamydomonas reinhardtii |
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| المؤلفون: | Le Moigne T., Sarti E., Nourisson A., Zaffagnini M., Carbone A., Lemaire S. D., Henri J. |
| المساهمون: | Le Moigne T., Sarti E., Nourisson A., Zaffagnini M., Carbone A., Lemaire S.D., Henri J. |
| سنة النشر: | 2022 |
| المجموعة: | IRIS Università degli Studi di Bologna (CRIS - Current Research Information System) |
| مصطلحات موضوعية: | Aldolase, Calvin-Benson-Bassham cycle, Carbon fixation, Enzyme, Functional classification, Photosynthesi, Post-translational modification, Redox, Structure, Carbon Dioxide, Chloroplast, Fructose, Fructose-Bisphosphate Aldolase, Ribulose-Bisphosphate Carboxylase, Chlamydomonas reinhardtii |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | ELETTRONICO |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/35680033; info:eu-repo/semantics/altIdentifier/wos/WOS:000822830400001; volume:214; issue:3; firstpage:107873; lastpage:107883; numberofpages:11; journal:JOURNAL OF STRUCTURAL BIOLOGY; https://hdl.handle.net/11585/912491Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85132716983 |
| DOI: | 10.1016/j.jsb.2022.107873 |
| الإتاحة: | https://doi.org/10.1016/j.jsb.2022.107873Test https://hdl.handle.net/11585/912491Test |
| رقم الانضمام: | edsbas.ACAD3F5C |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.jsb.2022.107873 |
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