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| - | [[Image:2bt9.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bt9| PDB=2bt9 | SCENE= }} | | {{STRUCTURE_2bt9| PDB=2bt9 | SCENE= }} |
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| - | '''LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH ME-FUCOSIDE'''
| + | ===LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH ME-FUCOSIDE=== |
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| - | ==Overview==
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| - | 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 x 10(-7) M for 2-fucosyllactose). R. solanacearum lectin has been crystallized with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with alpha-methyl-fucoside being at ultrahigh resolution, reveal that each monomer consists of two small four-stranded anti-parallel beta-sheets. Trimerization through a 3-fold or pseudo-3-fold axis generates a six-bladed beta-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a beta-propeller formed by oligomerization and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the beta-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharide from the primary cell wall of plants, which may be the biological target of the lectin.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15923179}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15923179 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15923179}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lectin]] | | [[Category: Lectin]] |
| | [[Category: Sugar recognition]] | | [[Category: Sugar recognition]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:46:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:25:47 2008'' |
Revision as of 18:25, 27 July 2008
Template:STRUCTURE 2bt9
LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH ME-FUCOSIDE
Template:ABSTRACT PUBMED 15923179
About this Structure
2BT9 is a Single protein structure of sequence from Ralstonia solanacearum. 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
Page seeded by OCA on Sun Jul 27 21:25:47 2008
