1w3f
From Proteopedia
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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 ... [(full description)]
About this Structure
1W3F is a [Single protein] structure of sequence from [Laetiporus sulphureus] with NLC and GOL as [ligands]. Structure known Active Site: AC1. 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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