Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00074228" target="_blank" >RIV/00216224:14740/14:00074228 - 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
Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies
Original language description
Photorhabdus luminescence is Gram-negative bacilli, exhibit duel nature of lifecycle one, being pathogenic towards insect whereas other, symbiosis with entamo-pathogenic nematodes. The lectin gene was amplified from the genome of P. luminescence and cloned with polyhistidine tag. Expression and production of the lectin was optimized and further purified it using nickel affinity chromatography. The lectin was found to be tetramer of 160 kDa exhibiting 41 kDa monomers interconnected with disulphide bridge. Crystallization of the lectin was achieved after various screening kits and optimized further by hanging drop method. The crystal structure was solved at 1.8 A resolution. The lectin was found to be seven-bladed beta-propeller fold with possibly two different binding sites per monomer. One of the binding site was found to be fucose specific however other was also suggested to be saccharide specificity probably towards a saccharide with higher level of hydroxylation than L-fucopyranose.
Czech name
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Czech description
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Project
<a href="/en/project/GA13-25401S" target="_blank" >GA13-25401S: Study of proteins from pathogens involved in host organism recognition</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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