Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae

Research output: Contribution to journalJournal articleResearchpeer-review

  • Molina, Rafael
  • Gonzalez, Ana Valeria
  • Meike Stelter
  • Inmaculada Pérez-Dorado
  • Richard Kahn
  • María Morales
  • Miriam Moscoso
  • Susana Campuzano
  • Nuria E Campillo
  • Shahriar Mobashery
  • José L García
  • Pedro García
  • Juan A Hermoso

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.

Original languageEnglish
JournalEMBO Reports
Issue number3
Pages (from-to)246-51
Number of pages6
Publication statusPublished - Mar 2009

    Research areas

  • 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

ID: 203019612