Complex carbohydrate recognition by proteins: Fundamental insights from bacteriophage cell adhesion systems

Protein–glycan interactions are ubiquitous in nature. Molecular description of complex formation and the underlying thermodynamics, however, are not well understood due to the lack of model systems. Bacteriophage tailspike proteins (TSP) possess binding sites for bacterial cell surfaces oligosacchar...

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Published inPerspectives in science Vol. 11; pp. 45 - 52
Main Authors Broeker, Nina K., Andres, Dorothee, Kang, Yu, Gohlke, Ulrich, Schmidt, Andreas, Kunstmann, Sonja, Santer, Mark, Barbirz, Stefanie
Format Journal Article
LanguageEnglish
Published Elsevier GmbH 01.01.2017
Subjects
Bacterial O-antigen
Carbohydrate interaction
Polysaccharide dynamics
Structural thermodynamics
Tailspike protein
TSP
RU
Tailspike protein
Bacterial O-antigen
ITC
Polysaccharide dynamics
Structural thermodynamics
Carbohydrate interaction
CBM
Online AccessGet full text
ISSN2213-0209
2213-0209
DOI10.1016/j.pisc.2016.10.001

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Abstract Protein–glycan interactions are ubiquitous in nature. Molecular description of complex formation and the underlying thermodynamics, however, are not well understood due to the lack of model systems. Bacteriophage tailspike proteins (TSP) possess binding sites for bacterial cell surfaces oligosaccharides. In this article we describe the analysis of TSP-oligosaccharide complexes. TSP provide large glycan interaction sites where affinity and specificity are guided by the protein surface solvation and the conformational space sampled by the respective glycan. Furthermore, we describe a computational approach to analyse the conformational space sampled by flexible glycans of bacterial origin, a prerequisite for a thorough understanding of TSP-oligosaccharide interactions.
AbstractList Protein–glycan interactions are ubiquitous in nature. Molecular description of complex formation and the underlying thermodynamics, however, are not well understood due to the lack of model systems. Bacteriophage tailspike proteins (TSP) possess binding sites for bacterial cell surfaces oligosaccharides. In this article we describe the analysis of TSP-oligosaccharide complexes. TSP provide large glycan interaction sites where affinity and specificity are guided by the protein surface solvation and the conformational space sampled by the respective glycan. Furthermore, we describe a computational approach to analyse the conformational space sampled by flexible glycans of bacterial origin, a prerequisite for a thorough understanding of TSP-oligosaccharide interactions.
Author Andres, Dorothee
Gohlke, Ulrich
Kang, Yu
Kunstmann, Sonja
Santer, Mark
Barbirz, Stefanie
Broeker, Nina K.
Schmidt, Andreas
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  givenname: Stefanie
  surname: Barbirz
  fullname: Barbirz, Stefanie
  email: barbirz@uni-potsdam.de
  organization: Physikalische Biochemie, Universität Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Golm, Germany
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Keywords TSP
RU
Tailspike protein
Bacterial O-antigen
ITC
Polysaccharide dynamics
Structural thermodynamics
Carbohydrate interaction
CBM
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Snippet Protein–glycan interactions are ubiquitous in nature. Molecular description of complex formation and the underlying thermodynamics, however, are not well...
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StartPage 45
SubjectTerms Bacterial O-antigen
Carbohydrate interaction
Polysaccharide dynamics
Structural thermodynamics
Tailspike protein
Title Complex carbohydrate recognition by proteins: Fundamental insights from bacteriophage cell adhesion systems
URI https://dx.doi.org/10.1016/j.pisc.2016.10.001
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