New family of bacterial lectins with seven bladed beta propeller fold

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Authors	SÝKOROVÁ Petra NOVOTNÁ Jitka DEMO Gabriel DEJMKOVÁ Eva KOMÁREK Jan HÁRONÍKOVÁ Lucia VARROT Annabelle IMBERTY Anne POKORNÁ Martina WIMMEROVÁ Michaela
Year of publication	2014
Type	Conference abstract
MU Faculty or unit	Central European Institute of Technology
Citation
Description	The crystal structures of BP39L and CV39L were determined based on a new class of lanthanide complexes for heavy atom derivatization (SAD experiment). The BP39L lectin crystallized in I222 space group and CV39L in P212121. The structures of both lectins revealed seven bladed beta propeller fold with possibly seven binding sites per monomer. The BP39L lectin was observed as a monomer and CV39L as a dimer in solution, which was confirmed also in the crystal structure. The knowledge about the structure together with sequence and structure predictions indicates that the proteins belong to an undescribed new family of lectins. The functional studies indicate the specificity of lectin BP39L towards mannose and CV39L towards fucose and galactose.
Related projects:	Studium proteinu z patogenu zapojených do rozpoznávání hostitelského organismu