Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO

被引:0
|
作者
Bjelcic, Monika [1 ]
Aurelius, Oskar [1 ]
Nan, Jie [1 ]
Neutze, Richard [2 ]
Ursby, Thomas [1 ]
机构
[1] Lund Univ, MAX IV Lab, POB 118, S-22100 Lund, Sweden
[2] Univ Gothenburg, Dept Chem & Mol Biol, Medicinaregatan 9C, S-41390 Gothenburg, Sweden
基金
瑞典研究理事会; 欧洲研究理事会; 欧盟地平线“2020”;
关键词
RuBisCO; SSX; serial synchrotron crystallography; room-temperature crystallography; spinach; Spinacia oleracea; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE-OXYGENASE; CRYSTAL-STRUCTURE; X-RAY; ACTIVATED RIBULOSE-1,5-BISPHOSPHATE; RIBULOSE 1,5-BISPHOSPHATE; RHODOSPIRILLUM-RUBRUM; HIGH-RESOLUTION; GREEN-ALGA; REFINEMENT; SUBSTRATE;
D O I
10.1107/S2053230X24004643
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Ribulose-1,5-bisphosphate carboxylase/ oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 angstrom resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
引用
收藏
页码:117 / 124
页数:8
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