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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| Authors: | N V Konareva A G Gabdulkhakov S Eschenburg S Stoeva A N Popov R Krauspenhaar M E Andrianova Yu Savochkina I I Agapov A G Tonevitskii A N Kornev V V Kornilov V N Zaitsev W Voelter Ch Betzel S V Nikonov B K Vainshtein A M Mikhailov |
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| Institution: | (1) Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 117333, Russia;(2) Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142292, Russia;(3) Institute of Physiological Chemistry, University Hospital, c/o DESY, Build. 22a, Notkestrasse 85, Hamburg, 22603, Germany;(4) Department of Physical Biochemistry, Institute of Physiological Chemistry, University of Tübingen, Hoppe-Seyler-Strasse 4, Tübingen, 72076, Germany;(5) State Research Center of Genetics and Selection of Industrial Microorganisms, VNIIGENETIKA, Pervyi Dorozhnyi proezd 1, Moscow, 113545, Russia;(6) Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow oblast, 142292, Russia |
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| 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. |
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