1W3A

Three dimensional structure of a novel pore-forming lectin from the mushroom Laetiporus sulphureus

Summary for 1W3A

• Entry DOI: 10.2210/pdb1w3a/pdb
• Related: 1W3F 1W3G
• Related PRD ID: PRD_900008
• Descriptor: HEMOLYTIC LECTIN LSLA, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• Functional Keywords: toxin, pore-forming toxin, hemolytic lectin, oligomer, beta-trefoil, sugar-binding protein, toxin-sugar binding protein complex, toxin/sugar binding protein
• Biological source: LAETIPORUS SULPHUREUS
• Total number of polymer chains: 1
• Total formula weight: 36019.82

Authors

Mancheno, J.M.,Tateno, H.,Goldstein, I.J.,Martinez-Ripoll, M.,Hermoso, J.A. (deposition date: 2004-07-14, release date: 2005-02-01, Last modification date: 2024-05-08)

Primary citation

Mancheno, J.M.,Tateno, H.,Goldstein, I.J.,Martinez-Ripoll, M.,Hermoso, J.A.
Structural Analysis of the Laetiporus Sulphureus Hemolytic Pore-Forming Lectin in Complex with Sugars
J.Biol.Chem., 280:17251-, 2005

PubMed Abstract: LSL is a lectin produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Here, we report the crystal structure of LSL refined to 2.6-A resolution determined by the single isomorphous replacement method with the anomalous scatter (SIRAS) signal of a platinum derivative. The structure reveals that LSL is hexameric, which was also shown by analytical ultracentrifugation. The monomeric protein (35 kDa) consists of two distinct modules: an N-terminal lectin module and a pore-forming module. The lectin module has a beta-trefoil scaffold that bears structural similarities to those present in toxins known to interact with galactose-related carbohydrates such as the hemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum, abrin, and ricin. On the other hand, the C-terminal pore-forming module (composed of domains 2 and 3) exhibits three-dimensional structural resemblances with domains 3 and 4 of the beta-pore-forming toxin aerolysin from the Gram-negative bacterium Aeromonas hydrophila, and domains 2 and 3 from the epsilon-toxin from Clostridium perfringens. This finding reveals the existence of common structural elements within the aerolysin-like family of toxins that could be directly involved in membrane-pore formation. The crystal structures of the complexes of LSL with lactose and N-acetyllactosamine reveal two dissacharide-binding sites per subunit and permits the identification of critical residues involved in sugar binding.

PubMed: 15687495
DOI: 10.1074/JBC.M413933200

Experimental method

X-RAY DIFFRACTION (2.65 Å)