Electron microscopy of the complexes of ribulose‐1,5‐bisphosphate carboxylase (Rubisco) and Rubisco subunit‐binding protein from pea leaves

FEBS Letters

Pushkin, A.V.²  Boekema, E.J.¹  Samsonidze, T.G.³  Tsuprun, V.L.³ 

[1] Biochemical Laboratory, Groningen University, Nijenborgh 16, 9747 AG Groningen, The Netherlands;A.N. Bach Institute of Biochemistry, USSR Academy of Sciences, Leninsky pr. 33, 117071 Moscow, USSR;A.V. Shubnikov Institute of Crystallography, USSR Academy of Sciences, Leninsky pr. 59, 117333 Moscow, USSR

关键词: Ribulose-1;    5-bisphosphate carboxylase (Rubisco);    Rubisco subunit-binding protein;    Quaternary structure;    Protein-protein complex;    Electron microscopy;   

DOI  :  10.1016/0014-5793(91)81070-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of ribulose-1,5-bisphosphate carboxylase (Rubisco) subunit-binding protein and its interaction with pea leaf chloroplast Rubisco were studied by electron microscopy and image analysis. Electron-microscopic evidence for the association of Rubisco subunit-binding protein, consisting of 14 subunits arranged with 72 point group symmetry, and oligomeric (L₈S₈) Rubisco was obtained.

【 授权许可】

Unknown