A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F15%3A00081460" target="_blank" >RIV/00216224:14310/15:00081460 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily
Original language description
The so-called ?PA-IIL lectin superfamily? includes several lectins from human opportunistic pathogens: PA-IIL (from Pseudomonas aeruginosa), CV-IIL (from Chromobacterium violaceum), BC2L-A and C-terminal domain from BC2L-C (from Burkholderia cenocepacia). Also, it includes one lectin from important plant pathogen: RS-IIL (from Ralstonia solanacearum). All these lectins are homologues with significant sequential and structural similarities but they differ in sugar-binding specificity. This fact is causedby differences in three amino acids which are arranged in the so-called ?specificity binding loop? (amino acids at positions 22-23-24). The previous study, which was focused on investigation of fine specificity of PA-IIL, confirmed that amino acid at position 22 is mainly responsible for sugar binding specificity. Specific amino acid substitution in this position led to change of sugar preference of PA-IIL to the RS-IIL one.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů