Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO

RuBisCO, D-ribulose-1,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis. In plants and some bacteria, this enzyme has an L8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The m...

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Bibliographic Details
Published in:Nature (London) 1987-09, Vol.329 (6137), p.354-356
Main Authors: Chapman, M.S, Suh, S.W, Cascio, D, Smith, W.W, Eisenberg, D
Format: Article
Language:English
Subjects:
Alcaligenes
Amino Acid Sequence
ANALISIS
ANALYSE
ANALYSIS
Binding Sites
Biological and medical sciences
Botany
Carbon dioxide
Crystalline structure
Crystallization
Enzymes
Flowers & plants
FOTOSINTESIS
Fundamental and applied biological sciences. Psychology
LIASAS
LYASE
LYASES
Macromolecular Substances
Molecular biophysics
Nicotiana - enzymology
NICOTIANA TABACUM
PHOTOSYNTHESE
PHOTOSYNTHESIS
Plants - enzymology
Plants, Toxic
Protein Conformation
RIBULOSE-BISPHOSPHATE CARBOXYLASE
Structure in molecular biology
Sugar
X RAY DIFFRACTION
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Summary:RuBisCO, D-ribulose-1,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis. In plants and some bacteria, this enzyme has an L8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 A along the 4-fold axis and 132 A in diameter at the widest point of the keg. Here we describe the quaternary structure of RuBisCO from N. tabacum, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution (3 A). The structure shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy. The structure, with its elongated and interdigitated L subunits, is evidence against a large, sliding-layer conformational change in plant RuBisCO, as proposed recently in Nature for the same enzyme from Alcaligenes eutrophus.
ISSN:0028-0836
1476-4687
DOI:10.1038/329354a0