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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate
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Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate

机译：结合核糖1,5-二磷酸核糖的豌豆的结构

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摘要

The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bisphosphate. X-ray diffraction data were recorded to 2.20 angstrom resolution from a single crystal at the Canadian Light Source. The overall quaternary structure of non-activated P. sativum Rubisco highlights the conservation of the form I Rubisco hexadecameric complex. The electron density places the substrate in the active site at the interface of the large-subunit dimers. Lys201 in the active site is not carbamylated as expected for this non-activated structure. Some heterogeneity in the small-subunit sequence is noted, as well as possible variations in the conformation and contacts of ribulose 1,5-bisphosphate in the large-subunit active sites. Overall, the active-site conformation most closely correlates with the 'closed' conformation observed in other substrate/inhibitor-bound Rubisco structures.
机译：报道了来自豆类作物的核糖-1，5-双磷酸羧化酶/加氧酶（Rubisco）的第一结构。 Rubisco是从豌豆（豌豆）中纯化得到的，在底物核糖1,5-双磷酸酯存在下，通过悬滴气相扩散获得了衍射级品质的晶体。来自加拿大光源的单晶X射线衍射数据记录为2.20埃分辨率。未活化的毕赤假单胞菌的整体四级结构突出了形式I鲁毕斯科六聚体的保守性。电子密度将底物置于大亚基二聚体界面的活性位点。活性位点中的Lys201未如未预期的那样被氨基甲酰化。注意到小亚基序列中的一些异质性，以及大亚基活性位点中核糖1,5-双磷酸核糖的构象和接触的可能变化。总体而言，活性位点构象与在其他底物/抑制剂结合的Rubisco结构中观察到的“封闭”构象最密切相关。

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