1xi0
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(New page: 200px<br /><applet load="1xi0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xi0, resolution 2.0Å" /> '''X-ray crystal structu...)
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Revision as of 00:03, 25 November 2007
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X-ray crystal structure of wild-type Xerocomus chrysenteron lectin XCL
Overview
A newly defined family of fungal lectins displays no significant sequence, similarity to any protein in the databases. These proteins, made of about, 140 amino acid residues, have sequence identities ranging from 38% to 65%, and share binding specificity to N-acetyl galactosamine. One member of, this family, the lectin XCL from Xerocomus chrysenteron, induces drastic, changes in the actin cytoskeleton after sugar binding at the cell surface, and internalization, and has potent insecticidal activity. The crystal, structure of XCL to 1.4 A resolution reveals the architecture of this new, lectin family. The fold of the protein is not related to any of the, several lectin folds documented so far. Unexpectedly, the structure, similarity is significant with actinoporins, a family of pore-forming, toxins. The specific structural features and sequence signatures in each, protein family suggest a potential sugar binding site in XCL and a, possible evolutionary relationship between these proteins. Finally, the, tetrameric assembly of XCL reveals a complex network of protomer-protomer, interfaces and generates a large, hydrated cavity of 1000 A3, which may, become accessible to larger solutes after a small conformational change of, the protein.
About this Structure
1XI0 is a Single protein structure of sequence from Xerocomus chrysenteron. Full crystallographic information is available from OCA.
Reference
A new lectin family with structure similarity to actinoporins revealed by the crystal structure of Xerocomus chrysenteron lectin XCL., Birck C, Damian L, Marty-Detraves C, Lougarre A, Schulze-Briese C, Koehl P, Fournier D, Paquereau L, Samama JP, J Mol Biol. 2004 Dec 10;344(5):1409-20. PMID:15561152
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