Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.
A three-dimensional crystal structure of the biotin-binding core of streptavidin has been determined at 3.1-A resolution. The structure was analyzed from diffraction data measured at three wavelengths from a single crystal of the selenobiotinyl complex with streptavidin. Streptavidin is a tetramer with subunits arrayed in D2 symmetry. Each protomer is an 8-stranded beta-barrel with simple up-down topology. Biotin molecules are bound at one end of each barrel. This study demonstrates the effectiveness of multiwavelength anomalous diffraction (MAD) procedures for macromolecular crystallography and provides a basis for detailed study of biotin-avidin interactions.
Hendrickson
W A
WA
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY.
Pähler
A
A
Smith
J L
JL
Satow
Y
Y
Merritt
E A
EA
Phizackerley
R P
RP
D001426:Bacterial Proteins; D001710:Biotin; D046911:Macromolecular Substances; D008958:Models, Molecular; D010315:Particle Accelerators; D011487:Protein Conformation; D012542:Scattering, Radiation; D013057:Spectrum Analysis; D019809:Streptavidin
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D001710:Biotin; D019809:Streptavidin