NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction.

TitleNMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction.
Publication TypeJournal Article
Year of Publication1995
AuthorsCasset, F., T. W. Hamelryck, R. Loris, J. R. Brisson, C. Tellier, M-H. Dao-Thi, L. Wyns, F. Poortmans, S. PĂ©rez, and A. Imberty
JournalJ Biol Chem
Volume270
Issue43
Pagination25619-28
Date Published1995 Oct 27
ISSN0021-9258
KeywordsComputer Simulation, Crystallography, X-Ray, Hydrogen Bonding, Lectins, Ligands, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Conformation, Plant Lectins, Sucrose
Abstract

The conformational features of sucrose in the combining site of lentil lectin have been characterized through elucidation of a crystalline complex at 1.9-A resolution, transferred nuclear Overhauser effect experiments performed at 600 Mhz, and molecular modeling. In the crystal, the lentil lectin dimer binds one sucrose molecule per monomer. The locations of 229 water molecules have been identified. NMR experiments have provided 11 transferred NOEs. In parallel, the docking study and conformational analysis of sucrose in the combining site of lentil lectin indicate that three different conformations can be accommodated. Of these, the orientation with lowest energy is identical with the one observed in the crystalline complex and provides good agreement with the observed transferred NOEs. These structural investigations indicate that the bound sucrose has a unique conformation for the glycosidic linkage, close to the one observed in crystalline sucrose, whereas the fructofuranose ring remains relatively flexible and does not exhibit any strong interaction with the protein. Major differences in the hydrogen bonding network of sucrose are found. None of the two inter-residue hydrogen bonds in crystalline sucrose are conserved in the complex with the lectin. Instead, a water molecule bridges hydroxyl groups O2-g and O3-f of sucrose.

Alternate JournalJ. Biol. Chem.
PubMed ID7592736