Structural highlights
Publication Abstract from PubMed
The choline-binding proteins play essential roles in pneumococcal colonization and virulence. It has been suggested that the choline-binding protein J (termed CbpJ; encoded by the gene sp_0378) from Streptococcus pneumoniae TIGR4 involves in the colonization in host and contributes to evasion of neutrophil killing. Here we report the 2.0A crystal structure of CbpJ in complex with choline. CbpJ consists of an N-terminal putative functional domain (N-domain) followed by a C-terminal choline-binding domain (CBD). The N-domain harbors four degenerated choline-binding repeats (CBRs) that lose the capacity of binding to choline, whereas the CBD is composed of seven typical CBRs. Further functional assays showed that the CBD contributes to the pneumococcal adhesion to human lung epithelial cell A549. These findings provide insights into the pneumococcal pathogenesis and broaden our understanding on the functions of choline-binding proteins.
Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae.,Xu Q, Zhang JW, Chen Y, Li Q, Jiang YL Biochem Biophys Res Commun. 2019 May 16. pii: S0006-291X(19)30921-0. doi:, 10.1016/j.bbrc.2019.05.053. PMID:31104766[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Q, Zhang JW, Chen Y, Li Q, Jiang YL. Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae. Biochem Biophys Res Commun. 2019 May 16. pii: S0006-291X(19)30921-0. doi:, 10.1016/j.bbrc.2019.05.053. PMID:31104766 doi:http://dx.doi.org/10.1016/j.bbrc.2019.05.053
