6gxr
Crystal structure of BP39L lectin from Burkholderia pseudomallei at 1.7 A resolutionCrystal structure of BP39L lectin from Burkholderia pseudomallei at 1.7 A resolution
Structural highlights
Publication Abstract from PubMedBurkholderia pseudomallei and Chromobacterium violaceum are bacteria of tropical and subtropical soil and water that occasionally cause fatal infections in humans and animals. Microbial lectins mediate the adhesion of organisms to host cells, which is the first phase in the development of infection. Here we report the discovery of two novel lectins from the above-mentioned bacteria - BP39L and CV39L. The crystal structures revealed that the lectins possess a seven-bladed beta-propeller fold. Functional studies conducted on a series of oligo- and polysaccharides confirmed the preference of BP39L for mannosylated saccharides and CV39L for rather more complex polysaccharides with a monosaccharide preference for beta-L-fucose. The presented data indicate that the proteins belong to a currently unknown family of lectins. Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed beta-propeller fold.,Sykorova P, Novotna J, Demo G, Pompidor G, Dubska E, Komarek J, Fujdiarova E, Houser J, Haronikova L, Varrot A, Shilova N, Imberty A, Bovin N, Pokorna M, Wimmerova M Int J Biol Macromol. 2019 Nov 18. pii: S0141-8130(19)33609-8. doi:, 10.1016/j.ijbiomac.2019.10.200. PMID:31751748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|