Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate

被引:50
作者
Mizohata, E
Matsumura, H
Okano, Y
Kumei, M
Takuma, H
Onodera, J
Kato, K
Shibata, N
Inoue, T
Yokota, A
Kai, Y
机构
[1] Osaka Univ, Grad Sch Engn, Dept Chem Mat, Osaka 5650871, Japan
[2] Nara Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300101, Japan
[3] Res Inst Innovat Technol Earth, Plant Mol Physiol Lab, Kizu, Kyoto 6190292, Japan
基金
日本学术振兴会;
关键词
rubisco; X-ray crystal structure; Chlamydomonas reinhardtii; post-translational modification; photosynthesis;
D O I
10.1006/jmbi.2001.5381
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyzes the initial steps of photosynthetic carbon reduction and photorespiratory carbon oxidation cycles by combining CO2 and O-2, respectively, with ribulose-1,5-bisphosphate. Many photosynthetic organisms have form 1 rubiscos comprised of eight large (L) and eight small (S) subunits. The crystal structure of the complex of activated rubisco from the green alga Chlamydomonas reinliardtii and the reaction intermediate analogue 2-carboxyarabinitol-1,5-bisphosphate (2-CABP) has been solved at 1.84 Angstrom resolution (R-cryst of 15.2% and R-free of 18.1%). The subunit arrangement of Chlamydomonas rubisco is the same as those of the previously solved form I rubiscos. Especially, the present structure is very similar to the activated spinach structure complexed with 2-CABP in the L-subunit folding and active-site conformation, but differs in S-subunit folding. The central insertion of the Chlamydomonas S-subunit forms the longer betaA-betaB loop that protrudes deeper into the solvent channel of rubisco than higher plant, cyanobacterial, and red algal (red-like) betaA-betaB loops. The C-terminal extension of the Chlamydomonas S-subunit does not protrude into the solvent channel, unlike that of the red algal S-subunit, but lies on the protein surface anchored by interactions with the N-terminal region of the S-subunit. Further, the present high-resolution structure has revealed novel post-translational modifications. Residue 1 of the S-subunit is N-alpha-methylmethionine, residues 104 and 151 of the L-subunit are 4-hydroxyproline, and residues 256 and 369 of the L-subunit are S-gamma-methylcysteine. Furthermore, the unusual electron density of residue 471 of the L-subunit, which has been deduced to be threonine from the genomic DNA sequence, suggests that the residue is isoleucine produced by RNA editing or O-gamma-methylthreonine. (C) 2002 Elsevier Science Ltd.
引用
收藏
页码:679 / 691
页数:13
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