Preliminary crystallographic characterization of ricin agglutinin.
The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 A x 60 A x 40 A with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-5 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.
Sweeney
E C
EC
Department of Crystallography, Birkbeck College, University of London, United Kingdom.
Tonevitsky
A G
AG
Temiakov
D E
DE
Agapov
I I
II
Saward
S
S
Palmer
R A
RA
D018360:Crystallography, X-Ray; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D037121:Plant Lectins; D011487:Protein Conformation
D037102:Lectins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1