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

Nature. 1987 Sep;329(6137):354-6. doi: 10.1038/329354a0.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallization
  • Macromolecular Substances
  • Nicotiana / enzymology
  • Plants / enzymology*
  • Plants, Toxic
  • Protein Conformation
  • Ribulose-Bisphosphate Carboxylase*
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Ribulose-Bisphosphate Carboxylase