A new Ralstonia solanacearum high affinity mannose-binding lectin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00009899" target="_blank" >RIV/00216224:14310/04:00009899 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
A new Ralstonia solanacearum high affinity mannose-binding lectin
Original language description
The plant pathogen Ralstonia solanacearum produces two lectins, each with different affinity for fucose. We described previously the properties and sequence of the first lectin, RSL (subunit Mr 9.9 kDa), that is related to fungal lectins (Sudakevitz, D.,Imberty, A., and Gilboa-Garber, N. (2002) J. Biochem. 132: 353-358). The present communication reports the discovery of the second one, RS-IIL (subunit Mr 11.6 kDa), a tetrameric lectin, with high sequence similarity to the fucose-binding lectin PA-IILof Pseudomanas aeruginosa. RS-IIL recognizes fucose but displays much higher affinity to mannose and fructose, which is opposite to the preference spectrum of PA-IIL. Determination of the crystal structure of RS-IIL complexed with a mannose derivative demonstrates a tetrameric structure very similar to the recently solved PA-IIL structure (Mitchell et al. (2002) Nature Struct. Biol. 9: 918-921). Each monomer contains two close calcium cations which mediate the binding of the monosacchari
Czech name
Nový manosu vázající lektin z Ralstonia solanacearum
Czech description
Nový manosu vázající lektin z Ralstonia solanacearum

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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