Three-dimensional structure of ubiquitin at 2.8 A resolution.
The three-dimensional structure of ubiquitin has been determined at 2.8 A resolution. X-ray diffraction data for the native protein and derivatives were collected with an automated diffractometer. Phases were obtained by use of a single isomorphous mercuric acetate derivative. The molecule contains a pronounced hydrophobic core. Prominent secondary structural features include three and one-half turns of alpha-helix, a mixed beta-sheet that contains four strands, and seven reverse turns. The histidine, tyrosine, and two phenylalanine residues are located on the surface of the molecule.
Vijay-Kumar
S
S
Bugg
C E
CE
Wilkinson
K D
KD
Cook
W J
WJ
D000595:Amino Acid Sequence; D006609:High Mobility Group Proteins; D006801:Humans; D046911:Macromolecular Substances; D008433:Mathematics; D008958:Models, Molecular; D014452:Ubiquitins; D014961:X-Ray Diffraction
D006609:High Mobility Group Proteins; D046911:Macromolecular Substances; D014452:Ubiquitins