8QJ0

Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO

Summary for 8QJ0

• Entry DOI: 10.2210/pdb8qj0/pdb
• Descriptor: Ribulose bisphosphate carboxylase small subunit, chloroplastic 2, Ribulose bisphosphate carboxylase large chain, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: spinacia oleracea, lyase
• Biological source: Spinacia oleracea (spinach); More
• Total number of polymer chains: 8
• Total formula weight: 270190.91

Authors

Bjelcic, M.,Neutze, R.,Aurelius, O.,Nan, J.,Ursby, T. (deposition date: 2023-09-12, release date: 2024-05-29, Last modification date: 2024-07-03)

Primary citation

Bjelcic, M.,Aurelius, O.,Nan, J.,Neutze, R.,Ursby, T.
Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO.
Acta Crystallogr.,Sect.F, 80:117-124, 2024

PubMed Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO) 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 CO by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 Å 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.

PubMed: 38809540
DOI: 10.1107/S2053230X24004643

Experimental method

X-RAY DIFFRACTION (2.3 Å)