TY - JOUR
T1 - Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO
AU - Chapman, Michael S.
AU - Suh, Se Won
AU - Cascio, Duilio
AU - Smith, Ward W.
AU - Eisenberg, David
PY - 1987
Y1 - 1987
N2 - RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 Å along the 4-fold axis and 132 Å in diameter at the widest point of the keg3-6. 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 Å). 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 microscopy5,6. The structure, with its elongated and inter-digitated 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 eutrophus7.
AB - RuBisCO, D-ribulose-l,5-bisphosphate carboxylase-oxygenase (EC 4.1.1.39), converts carbon dioxide to sugar in the first step of photosynthesis 1,2. In plants and some bacteria, this enzyme has an L 8S8 structure, where L is the large catalytic subunit and S is the small subunit of unknown function. The molecule resembles a keg 105 Å along the 4-fold axis and 132 Å in diameter at the widest point of the keg3-6. 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 Å). 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 microscopy5,6. The structure, with its elongated and inter-digitated 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 eutrophus7.
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U2 - 10.1038/329354a0
DO - 10.1038/329354a0
M3 - Article
C2 - 3627277
AN - SCOPUS:0023663713
SN - 0028-0836
VL - 329
SP - 354
EP - 356
JO - Nature
JF - Nature
IS - 6137
ER -