PortalPublikationenStructure analysis of endosialidase NF at 0.98 A resolution

Structure analysis of endosialidase NF at 0.98 A resolution

Standard

Structure analysis of endosialidase NF at 0.98 A resolution. / Schulz, Eike C; Neumann, Piotr; Gerardy-Schahn, Rita; Sheldrick, George M; Ficner, Ralf.

in: ACTA CRYSTALLOGR D, Jahrgang 66, Nr. Pt 2, 02.2010, S. 176-80.

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

Harvard

Schulz, EC, Neumann, P, Gerardy-Schahn, R, Sheldrick, GM & Ficner, R 2010, 'Structure analysis of endosialidase NF at 0.98 A resolution', ACTA CRYSTALLOGR D, Jg. 66, Nr. Pt 2, S. 176-80. https://doi.org/10.1107/S0907444909048720

APA

Schulz, E. C., Neumann, P., Gerardy-Schahn, R., Sheldrick, G. M., & Ficner, R. (2010). Structure analysis of endosialidase NF at 0.98 A resolution. ACTA CRYSTALLOGR D, 66(Pt 2), 176-80. https://doi.org/10.1107/S0907444909048720

Vancouver

Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R. Structure analysis of endosialidase NF at 0.98 A resolution. ACTA CRYSTALLOGR D. 2010 Feb;66(Pt 2):176-80. https://doi.org/10.1107/S0907444909048720

Bibtex

@article{e2b62e11b0f5457fab4dd2db155e5f10,
title = "Structure analysis of endosialidase NF at 0.98 A resolution",
abstract = "Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.",
keywords = "Bacteriophages/enzymology, Catalytic Domain, Crystallography, X-Ray, Enzyme Stability, Models, Molecular, N-Acetylneuraminic Acid/chemistry, Neuraminidase/chemistry, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary",
author = "Schulz, {Eike C} and Piotr Neumann and Rita Gerardy-Schahn and Sheldrick, {George M} and Ralf Ficner",
year = "2010",
month = feb,
doi = "10.1107/S0907444909048720",
language = "English",
volume = "66",
pages = "176--80",
journal = "ACTA CRYSTALLOGR D",
issn = "2059-7983",
publisher = "John Wiley and Sons Inc.",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - Structure analysis of endosialidase NF at 0.98 A resolution

AU - Schulz, Eike C

AU - Neumann, Piotr

AU - Gerardy-Schahn, Rita

AU - Sheldrick, George M

AU - Ficner, Ralf

PY - 2010/2

Y1 - 2010/2

N2 - Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.

AB - Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.

KW - Bacteriophages/enzymology

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Enzyme Stability

KW - Models, Molecular

KW - N-Acetylneuraminic Acid/chemistry

KW - Neuraminidase/chemistry

KW - Protein Multimerization

KW - Protein Structure, Quaternary

KW - Protein Structure, Tertiary

U2 - 10.1107/S0907444909048720

DO - 10.1107/S0907444909048720

M3 - SCORING: Journal article

C2 - 20124697

VL - 66

SP - 176

EP - 180

JO - ACTA CRYSTALLOGR D

JF - ACTA CRYSTALLOGR D

SN - 2059-7983

IS - Pt 2

ER -