PDBsum entry: 1apn

Lectin

PDB id: 1apn

Contents

Protein chains

224 a.a. *

Waters ×168

* Residue conservation analysis

PDB id:

1apn

Name:

Lectin

Title:

The crystallographic structure of metal-free concanavalin a at 2.5 angstroms resolution

Structure:

Concanavalin a. Chain: a, b. Synonym: con a. Other_details: demetallized, ph 5

Source:

Canavalia ensiformis. Jack bean. Organism_taxid: 3823

Biol. unit:

Tetramer (from PQS)

Resolution:

2.50Å R-factor: 0.180 R-free: 0.247

Authors:

J.Bouckaert,R.Loris,F.Poortmans,L.Wyns

Key ref:

J.Bouckaert et al. (1995). Crystallographic structure of metal-free concanavalin A at 2.5 A resolution. Proteins, 23, 510-524. PubMed id: 8749847 DOI: 10.1002/prot.340230406

Date:

28-Jul-95 Release date: 03-Apr-96

Protein chains

P02866  (CONA_CANEN) -  Concanavalin-A

Seq: 290 a.a.

Struc: 224 a.a.*

* PDB and UniProt seqs differ at 26 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biochemical function: binding (5 terms)

DOI no: 10.1002/prot.340230406

Proteins 23:510-524 (1995)

PubMed id: 8749847

Crystallographic structure of metal-free concanavalin A at 2.5 A resolution.

J.Bouckaert, R.Loris, F.Poortmans, L.Wyns.

ABSTRACT

The three-dimensional structure of demetallized concanavalin A has been determined at 2.5 A resolution and refined to a crystallographic R-factor of 18%. The lectin activity of concanavalin A requires the binding of both a transition metal ion, generally Mn2+, and a Ca2+ ion in two neighboring sites in close proximity to the carbohydrate binding site. Large structural differences between the native and the metal-free lectin are observed in the metal-binding region and consequently for the residues involved in the specific binding of saccharides. The demetallization invokes a series of conformational changes in the protein backbone, apparently initiated mainly by the loss of the calcium ion. Most of the Mn2+ ligands retain their position, but the Ca2+ binding site is destroyed. The Ala207-Asp208 peptide bond, in the beta-strand neighboring the metal-binding sites, undergoes a cis to trans isomerization. The cis conformation for this bond is a highly conserved feature among the leguminous lectins and is critically maintained by the Ca2+ ion in metal-bound concanavalin A. A further and major change adjacent to the isomerized bond is an expansion of the loop containing the monosaccharide ligand residues Leu99 and Tyr100. The dispersion of the ligand residues for the monosaccharide binding site (Asn14, Agr228, Asp208, Leu99, and Tyr100) in metal-free concanavalin A abolishes the lectin's ability to bind saccharides. Since the quaternary structure of legume lectins is essential to their biological role, the tetramer formation was analyzed. In the crystal (pH 5), the metal-free concanavalin A dimers associate into a tetramer that is similar to the native one, but with a drastically reduced number of inter-dimer interactions. This explains the tetramer dissociation into dimers below pH values of 6.5.