The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme.
The structure of complex I from Yarrowia lipolytica was determined by three-dimensional electron microscopy. A random conical data set was collected from deep stain embedded particles. More than 14000 image pairs were analyzed. Through extensive classification combined with three-dimensional reconstruction, it was possible for the first time to show a much more detailed substructure of the complex. The peripheral arm is subdivided in at least six domains. The membrane arm shows two major protrusions on its matrix facing side and exhibits a channel like feature on the side facing the cytoplasm. Structures resembling a tether connecting the subunits near the catalytic center with the protrusions of the membrane arm provide a second connection between matrix and membrane domain.
Radermacher
M
M
University of Vermont, College of Medicine, Department of Molecular Physiology and Biophysics, Burlington, VT, USA. Michael.Radermacher@uvm.edu
Ruiz
T
T
Clason
T
T
Benjamin
S
S
Brandt
U
U
Zickermann
V
V
D002462:Cell Membrane / Q000378:metabolism; D019295:Computational Biology / Q000379:methods; D003593:Cytoplasm / Q000378:metabolism; D042967:Electron Transport Complex I / Q000737:chemistry*; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D008968:Molecular Conformation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011886:Radon / Q000737:chemistry; D025062:Yarrowia / Q000201:enzymology*
D042967:Electron Transport Complex I; D011886:Radon