2WQ4

N-terminal domain of BC2L-C Lectin from Burkholderia cenocepacia

Summary for 2WQ4

• Entry DOI: 10.2210/pdb2wq4/pdb
• Descriptor: LECTIN, methyl 1-seleno-alpha-L-fucopyranoside, BROMIDE ION, ... (4 entities in total)
• Functional Keywords: lung, pathogen, infection, sugar binding protein
• Biological source: BURKHOLDERIA CENOCEPACIA
• Total number of polymer chains: 3
• Total formula weight: 48672.50

Authors

Sulak, O.,Cioci, G.,Lahman, M.,Delia, M.,Varrot, A.,Imberty, A.,Wimmerova, M. (deposition date: 2009-08-13, release date: 2010-01-12, Last modification date: 2024-10-16)

Primary citation

Sulak, O.,Cioci, G.,Lahman, M.,Delia, M.,Varrot, A.,Imberty, A.,Wimmerova, M.
A Tnf-Like Trimeric Lectin Domain from Burkholderia Cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
Structure, 18:59-, 2010

PubMed 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.

PubMed: 20152153
DOI: 10.1016/J.STR.2009.10.021

Experimental method

X-RAY DIFFRACTION (1.42 Å)