Rubisco forms a lattice inside alpha-carboxysomes.

Rubisco forms a lattice inside alpha-carboxysomes.
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DOI:
10.1038/s41467-022-32584-7
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发表时间:
2022-08-18
影响因子:
16.6
通讯作者:
--
中科院分区:
综合性期刊1区
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--
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尽管微区室在原核生物学和生物工程中的重要性,但结构异质性阻碍了对其结构、超微结构和空间组织的全面理解。在这里,我们采用冷冻电子断层扫描成像α-carboxysomes,一个假二十面体的微室负责碳固定。我们已经解决了一个高分辨率subtomography平均的Rubisco货物内的羧基,并确定了安排的酶。我们发现H. Neapolitanus Rubisco在体内聚合,由Rubisco小亚基介导。这些原纤维可以进一步压缩以形成具有六重伪对称性的晶格。这种排列保留了Rubisco活性位点周围的运动自由和可接近性,以及另外两种羧基体蛋白CsoSCA(一种碳酸酐酶)和无序CsoS 2的结合位点,即使Rubisco浓度超过800 μM。α-羧基体内Rubisco货物的这种表征提供了对微区室组织中有序与无序之间平衡的深入了解。许多自养细菌依靠Rubisco固定二氧化碳。在这里,作者报告了α-羧基体中Rubisco的位置、方向和结构;显示了它如何聚合并在这个隔间内形成晶格。
Despite the importance of microcompartments in prokaryotic biology and bioengineering, structural heterogeneity has prevented a complete understanding of their architecture, ultrastructure, and spatial organization. Here, we employ cryo-electron tomography to image α-carboxysomes, a pseudo-icosahedral microcompartment responsible for carbon fixation. We have solved a high-resolution subtomogram average of the Rubisco cargo inside the carboxysome, and determined the arrangement of the enzyme. We find that the H. neapolitanus Rubisco polymerizes in vivo, mediated by the small Rubisco subunit. These fibrils can further pack to form a lattice with six-fold pseudo-symmetry. This arrangement preserves freedom of motion and accessibility around the Rubisco active site and the binding sites for two other carboxysome proteins, CsoSCA (a carbonic anhydrase) and the disordered CsoS2, even at Rubisco concentrations exceeding 800 μM. This characterization of Rubisco cargo inside the α-carboxysome provides insight into the balance between order and disorder in microcompartment organization. Many autotrophic bacteria rely on Rubisco for carbon dioxide fixation. Here the authors report the position, orientation, and structure of Rubisco within alpha-carboxysomes; showing how it polymerizes and can form a lattice inside this compartment.
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