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Volume 271, Number 43, Issue of October 25, 1996 pp. 26449-26452
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Orderly Disposition of Heterogeneous Small Subunits in D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase from Spinach

(Received for publication, July 26, 1996, and in revised form, August 30, 1996)

Naoki Shibata , Tsuyoshi Inoue , Kazuhiro Fukuhara , Yoshitaka Nagara , Ryouichi Kitagawa , Shigeharu Harada , Nobutami Kasai , Koichi Uemura , Ko Kato , Akiho Yokota and Yasushi Kai

From the Department of Applied Chemistry, Faculty of Engineering, Osaka University, Suita, Osaka 565, Japan and  Plant Molecular Physiology Laboratory, Research Institute of Innovative Technology for the Earth, Soraku-gun, Kyoto 619-02, Japan

We determined the crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-Å resolution and found that the enzyme contained two kinds of S, SI and SII, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.


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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.