2V04

CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE

Summary for 2V04

• Entry DOI: 10.2210/pdb2v04/pdb
• Related: 2V05
• Descriptor: CHOLINE BINDING PROTEIN F, CHOLINE ION (3 entities in total)
• Functional Keywords: cbpf, choline-binding-protein, lipid-binding-protein, lipid binding protein
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 37052.14

Authors

Hermoso, J.,Molina, R.,Kahn, R.,Stelter, M. (deposition date: 2007-05-08, release date: 2008-06-10, Last modification date: 2024-05-08)

Primary citation

Molina, R.,Gonzalez, A.,Stelter, M.,Perez-Dorado, I.,Kahn, R.,Morales, M.,Campuzano, S.,Campillo, N.E.,Mobashery, S.,Garcia, J.L.,Garcia, P.,Hermoso, J.A.
Crystal Structure of Cbpf, a Bifunctional Choline-Binding Protein and Autolysis Regulator from Streptococcus Pneumoniae.
Embo Rep., 10:246-, 2009

PubMed 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.

PubMed: 19165143
DOI: 10.1038/EMBOR.2008.245

Experimental method

X-RAY DIFFRACTION (2.1 Å)