PDBsum entry 2c4d

Lectin

PDB id: 2c4d

Contents

Protein chain

401 a.a. *

Ligands

NAG ×6

SO4 ×4

Metals

_CA

Waters ×55

* Residue conservation analysis

PDB id:

2c4d

Name:

Lectin

Title:

2.6a crystal structure of psathyrella velutina lectin in complex with n-acetylglucosamine

Structure:

Psathyrella velutina lectin pvl. Chain: a

Source:

Psathyrella velutina. Organism_taxid: 71681. Other_details: wild mushroom

Resolution:

2.60Å R-factor: 0.205 R-free: 0.271

Authors:

G.Cioci,E.P.Mitchell,V.Chazalet,C.Gautier,S.Oscarson,H.Debray, S.Perez,A.Imberty

Key ref:

G.Cioci et al. (2006). Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium. J Mol Biol, 357, 1575-1591. PubMed id: 16497330 DOI: 10.1016/j.jmb.2006.01.066

Date:

18-Oct-05 Release date: 23-Jan-06

Protein chain

Q309D1  (Q309D1_9AGAR) -  Lectin PVL (Fragment) from Lacrymaria velutina

Seq: 395 a.a.

Struc: 401 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.jmb.2006.01.066

J Mol Biol 357:1575-1591 (2006)

PubMed id: 16497330

Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium.

G.Cioci, E.P.Mitchell, V.Chazalet, H.Debray, S.Oscarson, M.Lahmann, C.Gautier, C.Breton, S.Perez, A.Imberty.

ABSTRACT

The lectin from the mushroom Psathyrella velutina recognises specifically N-acetylglucosamine and N-acetylneuraminic acid containing glycans. The crystal structure of the 401 amino acid residue lectin shows that it adopts a very regular seven-bladed beta-propeller fold with the N-terminal region tucked into the central cavity around the pseudo 7-fold axis. In the complex with N-acetylglucosamine, six monosaccharides are bound in pockets located between two consecutive propeller blades. Due to the repeats shown by the sequence the binding sites are very similar. Five hydrogen bonds between the protein and the sugar hydroxyl and N-acetyl groups stabilize the complex, together with the hydrophobic interactions with a conserved tyrosine and histidine. The complex with N-acetylneuraminic acid shows molecular mimicry with the same hydrogen bond network, but with different orientations of the carbohydrate ring in the binding site. The beta-hairpin loops connecting the two inner beta-strands of each blade are metal binding sites and two to three calcium ions were located in the structure. The multispecificity and high multivalency of this mushroom lectin, combined with its similarity to the extracellular domain of an important class of cell adhesion molecules, integrins, are another example of the outstanding success of beta-propeller structures as molecular binding machines in nature.

Selected figure(s)

Figure 3.
Figure 3. Two orthogonal views of the crystal structure of native PVL. Calcium and chloride ions are represented by magenta and green spheres, respectively. Sulphate ions and 2-N-morpholino-ethanesulfonic acid (Mes) molecules are represented by capped sticks. Plots are made using Pymol (DeLano Scientific LLC), unless otherwise indicated.

Figure 6.
Figure 6. Two orthogonal views of the crystal structure of PVL complexed with GlcNAc. Calcium ions are represented by magenta spheres, sulphate ions and GlcNAc ligands by capped sticks.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 357, 1575-1591) copyright 2006.

Figures were selected by the author.