1w3a
From Proteopedia
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|PDB= 1w3a |SIZE=350|CAPTION= <scene name='initialview01'>1w3a</scene>, resolution 2.65Å | |PDB= 1w3a |SIZE=350|CAPTION= <scene name='initialview01'>1w3a</scene>, resolution 2.65Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LBT:LACTOSE'>LBT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3a OCA], [http://www.ebi.ac.uk/pdbsum/1w3a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w3a RCSB]</span> | ||
}} | }} | ||
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[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
[[Category: Tateno, H.]] | [[Category: Tateno, H.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: LBT]] | ||
[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
[[Category: hemolytic lectin]] | [[Category: hemolytic lectin]] | ||
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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 Mon Mar 31 00:30:33 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 2.65Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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