Structure of the TbBILBO1 N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch [Cell Biology]

December 20th, 2013 by Vidilaseris, K., Morriswood, B., Kontaxis, G., Dong, G.

TbBILBO1 is the only known component of the flagellar pocket collar, an essential cytoskeletal barrier element found in trypanosomes. The N-terminal domain (NTD) of TbBILBO1 was found to be dispensable for targeting of the protein in vivo. However, overexpression of constructs lacking the NTD caused complete growth inhibition, implying an essential requirement for this domain. A high-resolution structure of the NTD of TbBILBO1 showed that it forms a ubiquitin-like fold with a conserved surface patch. Mutagenesis of this patch recapitulated the phenotypic effects of deleting the entire domain, and was found to cause cell death. The surface patch on the NTD of TbBILBO1 is therefore a potential drug target.
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