| Literature DB >> 20152153 |
Ondrej Sulák1, Gianluca Cioci, Monia Delia, Martina Lahmann, Annabelle Varrot, Anne Imberty, Michaela Wimmerová.
Abstract
The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.Entities:
Mesh：
Substances：
Year: 2010 PMID： 20152153 DOI： 10.1016/j.str.2009.10.021
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006