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Título

Structural Analysis of the Laetiporus sulphureous Hemolytic Pore-forming Lectin in Complex with Sugars

AutorMancheño, Jose M. ; Hiroaki, Tateno; Goldstein, Irwin J.; Hermoso, Juan A.
Palabras claveLaetiporus sulphureus
Structural Analysis
Fecha de publicación29-abr-2005
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry (2005) 280, 17251-17259
ResumenLSL 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-Å 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 -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 -pore-forming toxin aerolysin from the Gram-negative bacterium Aeromonas hydrophila, and domains 2 and 3 from the -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.
Descripcióndisponible en: http://www.xtal.iqfr.csic.es/publications/jbc2005.pdf
Versión del editorhttp://dx.doi.org/10.1074/jbc.M413933200
URIhttp://hdl.handle.net/10261/12521
DOI10.1074/jbc.M413933200
ISSN0021-9258
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