1w3f

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[[Image:1w3f.gif|left|200px]]<br /><applet load="1w3f" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w3f.gif|left|200px]]
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caption="1w3f, resolution 2.58&Aring;" />
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'''CRYSTAL STRUCTURE OF THE HEMOLYTIC LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS COMPLEXED WITH N-ACETYLLACTOSAMINE IN THE GAMMA MOTIF'''<br />
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{{Structure
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|PDB= 1w3f |SIZE=350|CAPTION= <scene name='initialview01'>1w3f</scene>, resolution 2.58&Aring;
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|SITE= <scene name='pdbsite=AC1:Nlc+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NLC:2-(ACETYLAMINO)-2-DEOXY-4-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GLUCOPYRANOSE'>NLC</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE HEMOLYTIC LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS COMPLEXED WITH N-ACETYLLACTOSAMINE IN THE GAMMA MOTIF'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W3F 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=NLC:'>NLC</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Nlc+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3F OCA].
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1W3F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Laetiporus_sulphureus Laetiporus sulphureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3F OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15687495 15687495]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15687495 15687495]
[[Category: Laetiporus sulphureus]]
[[Category: Laetiporus sulphureus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pore-forming toxin]]
[[Category: pore-forming toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:51:37 2008''

Revision as of 12:51, 20 March 2008


PDB ID 1w3f

Drag the structure with the mouse to rotate
, resolution 2.58Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE HEMOLYTIC LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS COMPLEXED WITH N-ACETYLLACTOSAMINE IN THE GAMMA MOTIF


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

1W3F 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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