Physical and conformational properties of staphylokinase in solution.
The structure of staphylokinase has been analyzed by solution X-ray scattering, dynamic light scattering, ultracentrifugation and ultraviolet circular dichroism spectroscopy. Staphylokinase has a radius of gyration of 2.3 nm, a Stokes radius of 2.12 nm and a maximum dimension of 10 nm. The sedimentation coefficient is 1.71 S. These physical parameters indicate that the shape of staphylokinase is very elongated. The protein molecule consists of two folded domains of similar size. The mean distance of the centres of gravity of the domains is 3.7 nm. The mutual positions of the two domains are variable in solution. Thus, the molecule is shaped like a flexible dumbbell. About 18% of the amino acids of staphylokinase are organized in helical structures, 30% are incorporated in beta-sheets and 20% form turns.
Damaschun
G
G
Max Delbrück Centrum für Molekulare Medizin, Berlin-Buch, Germany.
Damaschun
H
H
Gast
K
K
Misselwitz
R
R
Zirwer
D
D
Gührs
K H
KH
Hartmann
M
M
Schlott
B
B
Triebel
H
H
Behnke
D
D
D002942:Circular Dichroism; D004926:Escherichia coli; D008027:Light; D008666:Metalloendopeptidases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D012996:Solutions; D013211:Staphylococcus aureus; D014461:Ultracentrifugation; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D012996:Solutions; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus