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Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF

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Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. / Schulz, Eike Christian; Schwarzer, David; Frank, Martin; Stummeyer, Katharina; Mühlenhoff, Martina; Dickmanns, Achim; Gerardy-Schahn, Rita; Ficner, Ralf.

in: J MOL BIOL, Jahrgang 397, Nr. 1, 19.03.2010, S. 341-51.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Schulz, EC, Schwarzer, D, Frank, M, Stummeyer, K, Mühlenhoff, M, Dickmanns, A, Gerardy-Schahn, R & Ficner, R 2010, 'Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF', J MOL BIOL, Jg. 397, Nr. 1, S. 341-51. https://doi.org/10.1016/j.jmb.2010.01.028

APA

Schulz, E. C., Schwarzer, D., Frank, M., Stummeyer, K., Mühlenhoff, M., Dickmanns, A., Gerardy-Schahn, R., & Ficner, R. (2010). Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. J MOL BIOL, 397(1), 341-51. https://doi.org/10.1016/j.jmb.2010.01.028

Vancouver

Schulz EC, Schwarzer D, Frank M, Stummeyer K, Mühlenhoff M, Dickmanns A et al. Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. J MOL BIOL. 2010 Mär 19;397(1):341-51. https://doi.org/10.1016/j.jmb.2010.01.028

Bibtex

@article{9b83ff08147c4be4bf59602b1a33b763,
title = "Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF",
abstract = "An alpha-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as Escherichia coli K1 and Neisseria meningitidis and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting E. coli K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia(3) molecule is bound in an extended conformation representing the enzyme-product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.",
keywords = "Bacteriophages/enzymology, Catalytic Domain, Crystallography, X-Ray, Glycoside Hydrolases, Models, Molecular, Mutant Proteins/chemistry, Neuraminidase/chemistry, Protein Structure, Secondary, Sialic Acids/metabolism, Substrate Specificity, Viral Tail Proteins/chemistry",
author = "Schulz, {Eike Christian} and David Schwarzer and Martin Frank and Katharina Stummeyer and Martina M{\"u}hlenhoff and Achim Dickmanns and Rita Gerardy-Schahn and Ralf Ficner",
note = "Copyright (c) 2010 Elsevier Ltd. All rights reserved.",
year = "2010",
month = mar,
day = "19",
doi = "10.1016/j.jmb.2010.01.028",
language = "English",
volume = "397",
pages = "341--51",
journal = "J MOL BIOL",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF

AU - Schulz, Eike Christian

AU - Schwarzer, David

AU - Frank, Martin

AU - Stummeyer, Katharina

AU - Mühlenhoff, Martina

AU - Dickmanns, Achim

AU - Gerardy-Schahn, Rita

AU - Ficner, Ralf

N1 - Copyright (c) 2010 Elsevier Ltd. All rights reserved.

PY - 2010/3/19

Y1 - 2010/3/19

N2 - An alpha-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as Escherichia coli K1 and Neisseria meningitidis and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting E. coli K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia(3) molecule is bound in an extended conformation representing the enzyme-product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.

AB - An alpha-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as Escherichia coli K1 and Neisseria meningitidis and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting E. coli K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia(3) molecule is bound in an extended conformation representing the enzyme-product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.

KW - Bacteriophages/enzymology

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Glycoside Hydrolases

KW - Models, Molecular

KW - Mutant Proteins/chemistry

KW - Neuraminidase/chemistry

KW - Protein Structure, Secondary

KW - Sialic Acids/metabolism

KW - Substrate Specificity

KW - Viral Tail Proteins/chemistry

U2 - 10.1016/j.jmb.2010.01.028

DO - 10.1016/j.jmb.2010.01.028

M3 - SCORING: Journal article

C2 - 20096705

VL - 397

SP - 341

EP - 351

JO - J MOL BIOL

JF - J MOL BIOL

SN - 0022-2836

IS - 1

ER -