Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae
Research output: Contribution to journal › Journal article › Research › peer-review
Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline-binding proteins. The three-dimensional structure of choline-binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non-consensus choline-binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well-defined modules. The carboxy-terminal module is involved in cell wall binding and the amino-terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis.
|Number of pages||6|
|Publication status||Published - Mar 2009|
- Amino Acid Sequence, Autolysis, Bacterial Proteins/chemistry, Choline/metabolism, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, N-Acetylmuramoyl-L-alanine Amidase/metabolism, Peptidoglycan/metabolism, Protein Structure, Tertiary, Receptors, Cell Surface/chemistry, Sequence Alignment, Streptococcus pneumoniae/genetics