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1w3g
From Proteopedia
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==Overview== | ==Overview== | ||
| - | LSL is a lectin produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Here, we report | + | 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== | ==About this Structure== | ||
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[[Category: Laetiporus sulphureus]] | [[Category: Laetiporus sulphureus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Goldstein, I | + | [[Category: Goldstein, I J.]] |
| - | [[Category: Hermoso, J | + | [[Category: Hermoso, J A.]] |
| - | [[Category: Mancheno, J | + | [[Category: Mancheno, J M.]] |
[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
[[Category: Tateno, H.]] | [[Category: Tateno, H.]] | ||
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[[Category: pore-forming toxin]] | [[Category: pore-forming toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:06 2008'' |
Revision as of 13:40, 21 February 2008
|
HEMOLYTIC LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS COMPLEXED WITH TWO N-ACETYLLACTOSAMINE MOLECULES.
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
1W3G 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 15:40:06 2008
