PDBsum entry 4z2q

Sugar binding protein

PDB id: 4z2q

Contents

Protein chains

141 a.a.

Ligands

TRS

NDG-NAG ×2

MPD ×2

Waters ×398

PDB id:

4z2q

Name:

Sugar binding protein

Title:

The crystal structure of sclerotium rolfsii lectin variant 1 (ssr1) in complex with n-acetyl-glucosamine

Structure:

Lectin. Chain: a, b. Engineered: yes

Source:

Athelia rolfsii. Organism_taxid: 39291. Gene: l1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.148 R-free: 0.186

Authors:

A.L.Kantsadi,V.I.Peppa,D.D.Leonidas

Key ref:

V.I.Peppa et al. (2015). Molecular Cloning, Carbohydrate Specificity and the Crystal Structure of Two Sclerotium rolfsii Lectin Variants. Molecules, 20, 10848-10865. PubMed id: 26076107 DOI: 10.3390/molecules200610848

Date:

30-Mar-15 Release date: 01-Jul-15

Protein chains

A0A0M3KL30  (A0A0M3KL30_9AGAM) -  Lectin from Athelia rolfsii

Seq: 141 a.a.

Struc: 141 a.a.

DOI no: 10.3390/molecules200610848

Molecules 20:10848-10865 (2015)

PubMed id: 26076107

Molecular Cloning, Carbohydrate Specificity and the Crystal Structure of Two Sclerotium rolfsii Lectin Variants.

V.I.Peppa, H.Venkat, A.L.Kantsadi, S.R.Inamdar, G.G.Bhat, S.Eligar, A.Shivanand, V.B.Chachadi, G.J.Satisha, B.M.Swamy, V.T.Skamnaki, S.E.Zographos, D.D.Leonidas.

ABSTRACT

SRL is a cell wall associated developmental-stage specific lectin secreted by Sclerotium rolfsii, a soil-born pathogenic fungus. SRL displays specificity for TF antigen (Galβ1→3GalNAc-α-Ser//Thr) expressed in all cancer types and has tumour suppressing effects in vivo. Considering the immense potential of SRL in cancer research, we have generated two variant gene constructs of SRL and expressed in E. coli to refine the sugar specificity and solubility by altering the surface charge. SSR1 and SSR2 are two different recombinant variants of SRL, both of which recognize TF antigen but only SSR1 binds to Tn antigen (GalNAcα-Ser/Thr). The glycan array analysis of the variants demonstrated that SSR1 recognizes TF antigen and their derivative with high affinity similar to SRL but showed highest affinity towards the sialylated Tn antigen, unlike SRL. The carbohydrate binding property of SSR2 remains unaltered compared to SRL. The crystal structures of the two variants were determined in free form and in complex with N-acetylglucosamine at 1.7 Å and 1.6 Å resolution, respectively. Structural analysis highlighted the structural basis of the fine carbohydrate specificity of the two SRL variants and results are in agreement with glycan array analysis.