Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin.


Abstract

Isothermal titration calorimetry measurements of the binding of 2'-fucosyllactose, lactose, N-acetyllactosamine, galactopyranose, 2-acetamido-2-deoxygalactopyranoside, methyl alpha-N-dansylgalactosaminide (Me-alpha-DNS-GalN), methyl alpha-D-galactopyranoside, methyl beta-D-galactopyranoside, and fucose to Erythrina corallodendron lectin (ECorL), a dimer with one binding site per subunit, were performed at 283-286 and 297-299 K. The site binding enthalpies, DeltaHb, with the exception of Me-alpha-DNS-GalN, are the same at both temperatures and range from -47.1 +/- 1.0 kJ mol-1 for N-acetyllactosamine to -4.4 +/- 0.3 kJ mol-1 for fucose, and the site binding constants range from 3.82 +/- 0.9 x 10(5)M-1 for Me-alpha-DNS-GalN at 283.2 K to 0.46 +/- 0.05 x 10(3) M-1 for fucose at 297.2 K. The binding reactions are mainly enthalpically driven except for fucose and exhibit enthalpy-entropy compensation. The binding enthalpies of the disaccharides are about twice the binding enthalpies of the monosaccharides in contrast to concanavalin A where the binding enthalpies do not double for the disaccharides. Differential scanning calorimetry measurements show that denaturation of the ECorL dimer results in dissociation into its monomer subunits. The binding constants from the increase in denaturation temperature of ECorL in the presence of saccharides are in agreement with values from isothermal titration calorimetry results. The thermal denaturation of ECorL occurs around 333 K, well below the 344-360 K denaturation temperature of other legume lectins of similar size and tertiary structure, undoubtedly due to the difference in its quaternary structure relative to other legume lectins. This is also apparent from the independent unfolding of its two domains. Study holds ProTherm entries: 5259 Extra Details: At scan rate=20Kh -1 binding site; enthalpy-entropy compensation; saccharides;,binding constants; domains

Submission Details

ID: bK3aTaFB3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:29 p.m.

Version: 1

Publication Details
Surolia A;Sharon N;Schwarz FP,J. Biol. Chem. (1996) Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin. PMID:8663419
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1GZC 2002-06-21 1.58 High-Resolution crystal structure of Erythrina cristagalli lectin in complex with lactose
1GZ9 2002-06-21 1.7 High-Resolution Crystal Structure of Erythrina cristagalli Lectin in Complex with 2'-alpha-L-Fucosyllactose
1AX0 1998-05-06 1.9 ERYTHRINA CORALLODENDRON LECTIN IN COMPLEX WITH N-ACTYLGALACTOSAMINE
1AXY 1998-05-06 1.95 ERYTHRINA CORALLODENDRON LECTIN
1AX1 1998-05-06 1.95 ERYTHRINA CORALLODENDRON LECTIN IN COMPLEX WITH LACTOSE
1AX2 1998-05-06 1.95 ERYTHRINA CORALLODENDRON LECTIN IN COMPLEX WITH N-ACETYLLACTOSAMINE
1AXZ 1998-05-06 1.95 ERYTHRINA CORALLODENDRON LECTIN IN COMPLEX WITH D-GALACTOSE
3N35 2011-03-30 2.0 Erythrina corallodendron lectin mutant (Y106G) with N-Acetylgalactosamine
1LTE 1994-01-31 2.0 STRUCTURE OF A LEGUME LECTIN WITH AN ORDERED N-LINKED CARBOHYDRATE IN COMPLEX WITH LACTOSE
3N3H 2011-03-30 2.0 Erythrina corallodendron lectin mutant (Y106G) in complex with citrate
3N36 2011-03-30 2.3 Erythrina corallodendron lectin mutant (Y106G) in complex with Galactose
1SFY 2004-08-10 2.55 Crystal structure of recombinant Erythrina corallodandron Lectin
1FYU 2000-10-25 2.6 Crystal structure of erythrina corallodendron lectin in hexagonal crystal form

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
96.7 Lectin P83410 LEC_ERYCG
100.0 Lectin P16404 LEC_ERYCO