2bt9
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(New page: 200px<br /> <applet load="2bt9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bt9, resolution 0.94Å" /> '''LECTIN FROM RALSTON...)
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Revision as of 19:53, 29 October 2007
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LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH ME-FUCOSIDE
Overview
Plant pathogens, like animal ones, use protein-carbohydrate interactions, in their strategy for host recognition, attachment, and invasion. The, bacterium Ralstonia solanacearum, which is distributed worldwide and, causes lethal wilt in many agricultural crops, was shown to produce a, potent L-fucose-binding lectin, R. solanacearum lectin, a small protein of, 90 amino acids with a tandem repeat in its amino acid sequence. In the, present study, surface plasmon resonance experiments conducted on a series, of oligosaccharides show a preference for binding to alphaFuc1-2Gal and, alphaFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the, presence of two binding sites per monomer and an unusually high affinity, of the lectin for alphaFuc1-2Gal-containing oligosaccharides (KD = 2.5 ... [(full description)]
About this Structure
2BT9 is a [Single protein] structure of sequence from [Ralstonia solanacearum] with MFU as [ligand]. Full crystallographic information is available from [OCA].
Reference
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan., Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A, J Biol Chem. 2005 Jul 29;280(30):27839-49. Epub 2005 May 27. PMID:15923179
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