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

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

doi:10.1038/embor.2008.245

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

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

Protein Structure and Function Program

38 Citations (Scopus)

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.

Original language	English
Journal	EMBO Reports
Volume	10
Issue number	3
Pages (from-to)	246-51
Number of pages	6
ISSN	1469-221X
DOIs	https://doi.org/10.1038/embor.2008.245
Publication status	Published - Mar 2009

Keywords

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

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Molina, R., González, A., Stelter, M., Pérez-Dorado, I., Kahn, R., Morales, M., Moscoso, M., Campuzano, S., Campillo, N. E., Mobashery, S., García, J. L., García, P., & Hermoso, J. A. (2009). Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae. EMBO Reports, 10(3), 246-51. https://doi.org/10.1038/embor.2008.245

Molina, R , González, A, Stelter, M, Pérez-Dorado, I, Kahn, R, Morales, M, Moscoso, M, Campuzano, S, Campillo, NE, Mobashery, S, García, JL, García, P & Hermoso, JA 2009, 'Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae', EMBO Reports, vol. 10, no. 3, pp. 246-51. https://doi.org/10.1038/embor.2008.245

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title = "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.",

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author = "Rafael Molina and Ana Gonz{\'a}lez and Meike Stelter and Inmaculada P{\'e}rez-Dorado and Richard Kahn and Mar{\'i}a Morales and Miriam Moscoso and Susana Campuzano and Campillo, {Nuria E} and Shahriar Mobashery and Garc{\'i}a, {Jos{\'e} L} and Pedro Garc{\'i}a and Hermoso, {Juan A}",

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doi = "10.1038/embor.2008.245",

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pages = "246--51",

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T1 - Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae

AU - Molina, Rafael

AU - González, Ana

AU - Stelter, Meike

AU - Pérez-Dorado, Inmaculada

AU - Kahn, Richard

AU - Morales, María

AU - Moscoso, Miriam

AU - Campuzano, Susana

AU - Campillo, Nuria E

AU - Mobashery, Shahriar

AU - García, José L

AU - García, Pedro

AU - Hermoso, Juan A

PY - 2009/3

Y1 - 2009/3

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Autolysis

KW - Bacterial Proteins/chemistry

KW - Choline/metabolism

KW - Crystallography, X-Ray

KW - Humans

KW - Models, Molecular

KW - Molecular Sequence Data

KW - N-Acetylmuramoyl-L-alanine Amidase/metabolism

KW - Peptidoglycan/metabolism

KW - Protein Structure, Tertiary

KW - Receptors, Cell Surface/chemistry

KW - Sequence Alignment

KW - Streptococcus pneumoniae/genetics

U2 - 10.1038/embor.2008.245

DO - 10.1038/embor.2008.245

M3 - Journal article

C2 - 19165143

SN - 1469-221X

VL - 10

SP - 246

EP - 251

JO - EMBO Reports

JF - EMBO Reports

IS - 3

ER -

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

Abstract

Keywords

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