The three-dimensional structure of the colicin E3 immunity protein by distance geometry calculation.
The three-dimensional solution structure of the colicin E3 immunity protein (84 residues) was determined by distance geometry calculations. The hydrophilic side of a four-stranded antiparallel beta-sheet constitutes a part of the surface of the protein, and two loops lie on the hydrophobic side of the sheet. All the three specificity-determining residues, which are included in the center of the beta-sheet, display their side groups on the protein surface.
Yajima
S
S
Department of Biotechnology, University of Tokyo, Japan.
Muto
Y
Y
Morikawa
S
S
Nakamura
H
H
Yokoyama
S
S
Masaki
H
H
Uozumi
T
T
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003087:Colicins / Q000037:antagonists & inhibitors*; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D003087:Colicins; D029968:Escherichia coli Proteins; C488855:ceiC protein, E coli; C007104:colicin immunity proteins