Fukosu vazajici lektin z Ralstonia solanacearum: novy typ beta barelu tvoreny oligomerizaci a interakce s fukosidem, fukosyllaktosou a rostlinnym xyloglukanem

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00013768" target="_blank" >RIV/00216224:14310/05:00013768 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The fucose-binding lectin from ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan

Popis výsledku v původním jazyce

Plant pathogens, as 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, RSL, 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 áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with á-methyl-fucoside being at ultra-high resolution, reveal that e

Název v anglickém jazyce

The fucose-binding lectin from ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan

Popis výsledku anglicky

Plant pathogens, as 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, RSL, 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 áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with á-methyl-fucoside being at ultra-high resolution, reveal that e

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

280

Číslo periodika v rámci svazku

30

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

27839-27849

Kód UT WoS článku

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EID výsledku v databázi Scopus

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