PDBsum entry 1gzc

Sugar binding protein

PDB id: 1gzc

Contents

Protein chain

239 a.a. *

Ligands

BGC-GAL

Metals

_CA

_MN

Waters ×266

* Residue conservation analysis

PDB id:

1gzc

Name:

Sugar binding protein

Title:

High-resolution crystal structure of erythrina cristagalli lectin in complex with lactose

Structure:

Erythrina crista-galli lectin. Chain: a

Source:

Erythrina crista-galli. Cockspur coral tree. Organism_taxid: 49817

Biol. unit:

Dimer (from PDB file)

Resolution:

1.58Å R-factor: 0.208 R-free: 0.226

Authors:

C.Svensson,U.Krengel

Key ref:

C.Svensson et al. (2002). High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2'-alpha-L-fucosyllactose and correlation with thermodynamic binding data. J Mol Biol, 321, 69-83. PubMed id: 12139934 DOI: 10.1016/S0022-2836(02)00554-5

Date:

17-May-02 Release date: 21-Jun-02

Protein chain

P83410  (LEC_ERYCG) -  Lectin from Erythrina crista-galli

Seq: 239 a.a.

Struc: 239 a.a.

DOI no: 10.1016/S0022-2836(02)00554-5

J Mol Biol 321:69-83 (2002)

PubMed id: 12139934

High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2'-alpha-L-fucosyllactose and correlation with thermodynamic binding data.

C.Svensson, S.Teneberg, C.L.Nilsson, A.Kjellberg, F.P.Schwarz, N.Sharon, U.Krengel.

ABSTRACT

The primary sequence of Erythrina cristagalli lectin (ECL) was mapped by mass spectrometry, and the crystal structures of the lectin in complex with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6A and 1.7A resolution, respectively. The two complexes were compared with the crystal structure of the closely related Erythrina corallodendron lectin (ECorL) in complex with lactose, with the crystal structure of the Ulex europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with two modeled complexes of ECorL with 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very similar to the crystal structure of ECL in complex with 2'-alpha-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity surrounded by Tyr106, Tyr108, Trp135 and Pro134 adjoining the primary combining site of the lectin. Marked differences were however noted between the models and the experimental structure in the network of hydrogen bonds and hydrophobic interactions holding the L-fucose in the combining site of the lectin, pointing to limitations of the modeling approach. In addition to the structural characterization of the ECL complexes, an effort was undertaken to correlate the structural data with thermodynamic data obtained from microcalorimetry, revealing the importance of the water network in the lectin combining site for carbohydrate binding.

Selected figure(s)

Figure 3.
Figure 3. Electron density for lactose (a) and fucosyllactose (b), in the respective ECL complexes. 2F[o] -F[c] simulated-annealing omit maps covering the saccharides, displayed at 1s.

Figure 4.
Figure 4. Topology of ECL (complex with lactose). ECL residues that differ from ECorL are shown explicity. In addition, Val 92, the interaction partner of residues 111 and 125, is highlighted in orange.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 321, 69-83) copyright 2002.

Figures were selected by the author.