1w3a
From Proteopedia
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| - | [[Image:1w3a.gif|left|200px]]<br /><applet load="1w3a" size=" | + | [[Image:1w3a.gif|left|200px]]<br /><applet load="1w3a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w3a, resolution 2.65Å" /> | caption="1w3a, resolution 2.65Å" /> | ||
'''THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS'''<br /> | '''THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laetiporus_sulphureus Laetiporus sulphureus] with LBT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1W3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laetiporus_sulphureus Laetiporus sulphureus] with <scene name='pdbligand=LBT:'>LBT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pore-forming toxin]] | [[Category: pore-forming toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:18:47 2008'' |
Revision as of 08:18, 3 February 2008
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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 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
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