The three-dimensional structure of the regular surface protein of Comamonas acidovorans derived from native outer membranes and reconstituted two-dimensional crystals.
The three-dimensional structure of the regular surface protein (p4 symmetry, lattice constant a = b = 10.5 nm) of Comamonas acidovorans has been determined to a resolution of about 1.5 nm by means of electron microscopy and image processing. Three-dimensional reconstructions were performed using native outer membranes and artificial two-dimensional crystals of the surface protein, which was selectively solubilized by deoxycholate and recrystallized on carbon films. The two-fold symmetric morphological complex is composed of two identical monomers which are in tight contact with the outer membrane and presumably anchored to it by a small hydrophobic domain.
Engelhardt
H
H
Max-Plank-Institute für Biochemie, Martinsried, Germany.
Gerbl-Rieger
S
S
Santarius
U
U
Baumeister
W
W
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D007091:Image Processing, Computer-Assisted; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry*; D008854:Microscopy, Electron; D008958:Models, Molecular; D018272:Porins; D011487:Protein Conformation; D011549:Pseudomonas / Q000648:ultrastructure; D013194:Staining and Labeling
D001425:Bacterial Outer Membrane Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D018272:Porins