This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1w3f
From Proteopedia
|
CRYSTAL STRUCTURE OF THE HEMOLYTIC LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS COMPLEXED WITH N-ACETYLLACTOSAMINE IN THE GAMMA MOTIF
Overview
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.
About this Structure
1W3F is a Single protein structure of sequence from Laetiporus sulphureus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars., Mancheno JM, Tateno H, Goldstein IJ, Martinez-Ripoll M, Hermoso JA, J Biol Chem. 2005 Apr 29;280(17):17251-9. Epub 2005 Feb 1. PMID:15687495
Page seeded by OCA on Thu Feb 21 15:40:01 2008
