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

Abstract

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.

• Authors: Rafael Molina, Ana González, 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
• Journal: EMBO reports (EMBO Rep) Vol. 10 Issue 3 Pg. 246-51 (Mar 2009) ISSN: 1469-3178 [Electronic] England
• PMID: 19165143 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Peptidoglycan
• Receptors, Cell Surface
• LytC protein, Streptococcus
• N-Acetylmuramoyl-L-alanine Amidase
• Choline

Topics

• Amino Acid Sequence
• Autolysis
• Bacterial Proteins (chemistry, genetics, metabolism)
• 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, genetics, metabolism)
• Sequence Alignment
• Streptococcus pneumoniae (genetics, metabolism)