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-Structure paper
タイトル | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX. |
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ジャーナル・号・ページ | Cell Discov, Vol. 8, Issue 1, Page 93, Year 2022 |
掲載日 | 2022年9月20日 |
![]() | Qiong Li / Yong-Liang Jiang / Ling-Yun Xia / Yuxing Chen / Cong-Zhao Zhou / ![]() |
PubMed 要旨 | RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series ...RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series of chaperones that include RbcX and RuBisCO accumulation factor 1 (Raf1). To understand how these RuBisCO-specific chaperones function during cyanobacterial RbcLRbcS (LS) holoenzyme formation, we solved a 3.3-Å cryo-electron microscopy structure of a 32-subunit RbcLRaf1RbcX (LFX) assembly intermediate from Anabaena sp. PCC 7120. Comparison to the previously resolved LF and LX structures together with biochemical assays revealed that the LFX complex forms a rather dynamic structural intermediate, favoring RbcS displacement of Raf1 and RbcX. In vitro assays further demonstrated that both Raf1 and RbcX function to regulate RuBisCO condensate formation by restricting CcmM35 binding to the stably assembled LS holoenzymes. Combined with previous findings, we propose a model on how Raf1 and RbcX work in concert to facilitate, and regulate, cyanobacterial RuBisCO assembly as well as disassembly of RuBisCO condensates. |
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手法 | EM (単粒子) |
解像度 | 3.3 Å |
構造データ | EMDB-33524: Cryo-EM strutcure of a assembly intermediate RbcL8Raf18RbcX16 |
由来 |
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![]() | PHOTOSYNTHESIS / RuBisCO intermediate |