Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin.


Abstract

Soybean agglutinin (gSBA) is a tetrameric legume lectin, each of whose subunits are glycosylated. Earlier studies have shown that this protein shows exceptionally high stability in terms of free energy of unfolding when compared to other proteins from the same family. This article deals with the unfolding reactions of the nonglycosylated recombinant form of the protein rSBA and its comparison with the glycosylated counterpart gSBA. The nonglycosylated form features a lower stability when compared to the glycosylated form. Further, the unfolding pathways in the two are widely different. Although the glycosylated form undergoes a simple two-state unfolding, the nonglycosylated species unfolds via a compact monomeric intermediate that is not a molten globule. Representative isothermal and thermal denaturation profiles show that glycosylation accounts for a stabilization of approximately 9 kcal/mol of the tetramer, whereas the difference in T(m) between the two forms is 26 degrees C. Computational studies on the glycan-protein interactions at the noncanonical interface of the protein show that quite a number of hydrogen bond and hydrophobic interactions stabilize the glycoprotein tetramer. Study holds ProTherm entries: 23660, 23661 Extra Details: recombinant form glycosylated; recombinant; two-state unfolding; glycan-protein interactions

Submission Details

ID: M3sZa4jM4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:54 p.m.

Version: 1

Publication Details
Sinha S;Surolia A,Biophys. J. (2007) Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin. PMID:16980353
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
1SBF 1998-04-22 2.43 SOYBEAN AGGLUTININ
1G9F 2001-06-13 2.5 CRYSTAL STRUCTURE OF THE SOYBEAN AGGLUTININ IN A COMPLEX WITH A BIANTENNARY BLOOD GROUP ANTIGEN ANALOG
1SBD 1998-04-22 2.52 SOYBEAN AGGLUTININ COMPLEXED WITH 2,4-PENTASACCHARIDE
2SBA 1998-12-09 2.6 SOYBEAN AGGLUTININ COMPLEXED WITH 2,6-PENTASACCHARIDE
4D69 2014-11-19 2.7 SOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN Tn
1SBE 1998-04-22 2.8 SOYBEAN AGGLUTININ FROM GLYCINE MAX

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Lectin P05046 LEC_SOYBN