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Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO

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Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. / Schulz, Eike C; Bergfeld, Anne K; Ficner, Ralf; Mühlenhoff, Martina.

In: PLOS ONE, Vol. 6, No. 3, 01.03.2011, p. e17403.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schulz, EC, Bergfeld, AK, Ficner, R & Mühlenhoff, M 2011, 'Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO', PLOS ONE, vol. 6, no. 3, pp. e17403. https://doi.org/10.1371/journal.pone.0017403

APA

Schulz, E. C., Bergfeld, A. K., Ficner, R., & Mühlenhoff, M. (2011). Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. PLOS ONE, 6(3), e17403. https://doi.org/10.1371/journal.pone.0017403

Vancouver

Schulz EC, Bergfeld AK, Ficner R, Mühlenhoff M. Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. PLOS ONE. 2011 Mar 1;6(3):e17403. https://doi.org/10.1371/journal.pone.0017403

Bibtex

@article{b53805e3eb4742cb9441db8e38f16649,
title = "Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO",
abstract = "The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of α2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed β-helix (LβH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LβH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-ψ-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-ψ-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme.",
keywords = "Acetyltransferases/chemistry, Amino Acid Sequence, Biocatalysis, Catalytic Domain, Crystallography, X-Ray, Escherichia coli/enzymology, Escherichia coli Proteins/chemistry, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Sialic Acids/metabolism, Structural Homology, Protein, Substrate Specificity",
author = "Schulz, {Eike C} and Bergfeld, {Anne K} and Ralf Ficner and Martina M{\"u}hlenhoff",
year = "2011",
month = mar,
day = "1",
doi = "10.1371/journal.pone.0017403",
language = "English",
volume = "6",
pages = "e17403",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "3",

}

RIS

TY - JOUR

T1 - Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO

AU - Schulz, Eike C

AU - Bergfeld, Anne K

AU - Ficner, Ralf

AU - Mühlenhoff, Martina

PY - 2011/3/1

Y1 - 2011/3/1

N2 - The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of α2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed β-helix (LβH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LβH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-ψ-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-ψ-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme.

AB - The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of α2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed β-helix (LβH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LβH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-ψ-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-ψ-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme.

KW - Acetyltransferases/chemistry

KW - Amino Acid Sequence

KW - Biocatalysis

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Escherichia coli/enzymology

KW - Escherichia coli Proteins/chemistry

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Structure, Tertiary

KW - Sialic Acids/metabolism

KW - Structural Homology, Protein

KW - Substrate Specificity

U2 - 10.1371/journal.pone.0017403

DO - 10.1371/journal.pone.0017403

M3 - SCORING: Journal article

C2 - 21390252

VL - 6

SP - e17403

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 3

ER -