6JYX

Structure of CbpJ from Streptococcus Pneumoniae TIGR4

Summary for 6JYX

• Entry DOI: 10.2210/pdb6jyx/pdb
• Descriptor: Choline binding protein J, CHOLINE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: streptococcus pneumoniae, choline-binding proteins, adhesion, choline-binding protein
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 2
• Total formula weight: 73244.70

Authors

Xu, Q.,Zhang, J.W.,Li, Q.,Jiang, Y.L. (deposition date: 2019-04-29, release date: 2019-06-05, Last modification date: 2023-11-22)

Primary citation

Xu, Q.,Zhang, J.W.,Chen, Y.,Li, Q.,Jiang, Y.L.
Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae.
Biochem.Biophys.Res.Commun., 514:1192-1197, 2019

PubMed Abstract: 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 2.0 Å 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.

PubMed: 31104766
DOI: 10.1016/j.bbrc.2019.05.053

Experimental method

X-RAY DIFFRACTION (2 Å)