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Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with β-D-galactose in the crystalline state

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Eschenburg,  Susanne
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Konareva, N. V., Gabdulkhakov, A. G., Eschenburg, S., Stoeva, S., Popov, A. N., Krauspenhaar, R., et al. (2001). Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with β-D-galactose in the crystalline state. Crystallography Reports, 46(5), 792-800. doi:10.1134/1.1405866.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-F120-8
Abstract
The three-dimensional structure of the complex of agglutinin from Ricinus communis with β-D-galactose was established and refined at 2.5 Å resolution by X-ray structure analysis. Biocrystals were obtained using dialysis through a semipermeable membrane. X-ray intensity data (R merge = 4.6%) were collected from one crystal at 100 K using synchrotron radiation at the DESY outstation [European Molecular Biology Laboratory (EMBL), Hamburg, Germany]. The initial phases were calculated by the molecular replacement method. The atoms of both protein and sugar molecules were localized. Unlike ricin, the ricinlike heterodimer RcA contains only one galactose-binding center in the region of the Asn46-Gly25-Trp37-Lys40 site in the first domain of the B subunit, whereas the second galactose-binding site of the B subunit is lost. One functionally important water molecule, which is bound to the residues Tyr123-Glu176-Arg179-Glu207, was revealed in the region of the active center in the A subunit.