1w3a
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1w3a.gif|left|200px]] | [[Image:1w3a.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1w3a", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1w3a| PDB=1w3a | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS''' | '''THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS''' | ||
| Line 30: | Line 27: | ||
[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
[[Category: Tateno, H.]] | [[Category: Tateno, H.]] | ||
| - | [[Category: | + | [[Category: Beta-trefoil]] |
| - | [[Category: | + | [[Category: Hemolytic lectin]] |
| - | [[Category: | + | [[Category: Oligomer]] |
| - | [[Category: | + | [[Category: Pore-forming toxin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:05:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:05, 3 May 2008
THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS
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
1W3A is a Single protein structure of sequence from Laetiporus sulphureus. 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 Sat May 3 13:05:51 2008
