A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00088341" target="_blank" >RIV/00216224:14740/16:00088341 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.jbc.org/content/291/48/25032" target="_blank" >http://www.jbc.org/content/291/48/25032</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M115.693473" target="_blank" >10.1074/jbc.M115.693473</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure

Popis výsledku v původním jazyce

Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity toward insect larvae. Ahypothetical protein from P. luminescens was identified, purified from the native source, and characterized as an L-fucose-binding lectin, named P. luminescens lectin (PLL). Glycan array and biochemical characterization data revealed PLL to be specific toward L-fucose and the disaccharide glycan 3,6-O-Me-2-Glc beta 1-4(2,3-O-Me-2)Rha alpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homotetramer with an intersubunit disulfide bridge. The crystal structures of native and recombinant PLL revealed a seven-bladed beta-propeller fold creating seven putative fucose-binding sites per monomer. The crystal structure of the recombinant PLL.L-fucose complex confirmed that at least three sites were fucose-binding.

Název v anglickém jazyce

A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure

Popis výsledku anglicky

Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity toward insect larvae. Ahypothetical protein from P. luminescens was identified, purified from the native source, and characterized as an L-fucose-binding lectin, named P. luminescens lectin (PLL). Glycan array and biochemical characterization data revealed PLL to be specific toward L-fucose and the disaccharide glycan 3,6-O-Me-2-Glc beta 1-4(2,3-O-Me-2)Rha alpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homotetramer with an intersubunit disulfide bridge. The crystal structures of native and recombinant PLL revealed a seven-bladed beta-propeller fold creating seven putative fucose-binding sites per monomer. The crystal structure of the recombinant PLL.L-fucose complex confirmed that at least three sites were fucose-binding.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

The Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

291

Číslo periodika v rámci svazku

48

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

18

Strana od-do

25032-25049

Kód UT WoS článku

000388880100020

EID výsledku v databázi Scopus

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