NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction: J.Biol.Chem.

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TypeArticle
Journal titleJ.Biol.Chem.
Volume270
Issue43
Pages2561925628; # of pages: 10
Subjectanalysis; BOND; chemistry; Comparative Study; complex; COMPLEXES; Computer Simulation; conformation; CONFORMATIONAL; conformational analysis; CONFORMATIONAL-ANALYSIS; CONFORMATIONS; crystal; Crystallography,X-Ray; DIFFERENCE; ELUCIDATION; ENERGY; Hydrogen; Hydrogen Bonding; interaction; lectin; Lectins; LIGAND; Ligands; LOCATION; Magnetic Resonance Spectroscopy; Models,Molecular; MOLECULAR; Molecular Conformation; MOLECULE; NMR; NOE; NUCLEAR; Orientation; OVERHAUSER; Plant Lectins; protein; RESOLUTION; RING; SITE; STRUCTURAL; STRUCTURAL INVESTIGATIONS; Sucrose; Support,Non-U.S.Gov't; transferred; transferred NOE; Water
AbstractThe 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
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberCASSET1995A
NPARC number9367454
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Record identifiercbcc5f83-e350-46bf-9c96-30b4a4eb949a
Record created2009-07-10
Record modified2016-05-09
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