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6GXS

Crystal structure of CV39L lectin from Chromobacterium violaceum at 1.8 A resolution

Summary for 6GXS
Entry DOI10.2210/pdb6gxs/pdb
DescriptorCV39L lectin, SULFATE ION, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordslectin, sugar binding protein
Biological sourceChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Total number of polymer chains4
Total formula weight160982.28
Authors
Sykorova, P.,Novotna, J.,Demo, G.,Pompidor, G.,Dubska, E.,Komarek, J.,Fujdiarova, E.,Haronikova, L.,Varrot, A.,Imberty, A.,Shilova, N.,Bovin, N.,Pokorna, M.,Wimmerova, M. (deposition date: 2018-06-27, release date: 2019-12-04, Last modification date: 2024-05-15)
Primary citationSykorova, 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.
Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed beta-propeller fold.
Int.J.Biol.Macromol., 152:1113-1124, 2020
Cited by
PubMed Abstract: Burkholderia 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 β-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 β-l-fucose. The presented data indicate that the proteins belong to a currently unknown family of lectins.
PubMed: 31751748
DOI: 10.1016/j.ijbiomac.2019.10.200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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