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Structure analysis of Entamoeba histolytica enolase

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Structure analysis of Entamoeba histolytica enolase. / Schulz, Eike C; Tietzel, Michael; Tovy, Ayala; Ankri, Serge; Ficner, Ralf.

in: ACTA CRYSTALLOGR D, Jahrgang 67, Nr. Pt 7, 07.2011, S. 619-27.

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

Harvard

Schulz, EC, Tietzel, M, Tovy, A, Ankri, S & Ficner, R 2011, 'Structure analysis of Entamoeba histolytica enolase', ACTA CRYSTALLOGR D, Jg. 67, Nr. Pt 7, S. 619-27. https://doi.org/10.1107/S0907444911016544

APA

Schulz, E. C., Tietzel, M., Tovy, A., Ankri, S., & Ficner, R. (2011). Structure analysis of Entamoeba histolytica enolase. ACTA CRYSTALLOGR D, 67(Pt 7), 619-27. https://doi.org/10.1107/S0907444911016544

Vancouver

Schulz EC, Tietzel M, Tovy A, Ankri S, Ficner R. Structure analysis of Entamoeba histolytica enolase. ACTA CRYSTALLOGR D. 2011 Jul;67(Pt 7):619-27. https://doi.org/10.1107/S0907444911016544

Bibtex

@article{9544c581e3984b2799221a439bef43e8,
title = "Structure analysis of Entamoeba histolytica enolase",
abstract = "Entamoeba histolytica enolase (EhENO) reversibly interconverts 2-phosphoglyceric acid (2-PGA) and phosphoenolpyruvic acid (PEP). The crystal structure of the homodimeric EhENO is presented at a resolution of 1.9 {\AA}. In the crystal structure EhENO presents as an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation. Interestingly, both active sites contain a copurified 2-PGA molecule. While the 2-PGA molecule in the closed active site closely resembles the conformation known from other enolase-2-PGA complexes, the conformation in the open active site is different. Here, 2-PGA is shifted approximately 1.6 {\AA} away from metal ion I, most likely representing a precatalytic situation.",
keywords = "Crystallography, X-Ray, Entamoeba histolytica/enzymology, Humans, Models, Molecular, Phosphopyruvate Hydratase/chemistry, Protein Structure, Quaternary, Protein Structure, Tertiary",
author = "Schulz, {Eike C} and Michael Tietzel and Ayala Tovy and Serge Ankri and Ralf Ficner",
year = "2011",
month = jul,
doi = "10.1107/S0907444911016544",
language = "English",
volume = "67",
pages = "619--27",
journal = "ACTA CRYSTALLOGR D",
issn = "2059-7983",
publisher = "John Wiley and Sons Inc.",
number = "Pt 7",

}

RIS

TY - JOUR

T1 - Structure analysis of Entamoeba histolytica enolase

AU - Schulz, Eike C

AU - Tietzel, Michael

AU - Tovy, Ayala

AU - Ankri, Serge

AU - Ficner, Ralf

PY - 2011/7

Y1 - 2011/7

N2 - Entamoeba histolytica enolase (EhENO) reversibly interconverts 2-phosphoglyceric acid (2-PGA) and phosphoenolpyruvic acid (PEP). The crystal structure of the homodimeric EhENO is presented at a resolution of 1.9 Å. In the crystal structure EhENO presents as an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation. Interestingly, both active sites contain a copurified 2-PGA molecule. While the 2-PGA molecule in the closed active site closely resembles the conformation known from other enolase-2-PGA complexes, the conformation in the open active site is different. Here, 2-PGA is shifted approximately 1.6 Å away from metal ion I, most likely representing a precatalytic situation.

AB - Entamoeba histolytica enolase (EhENO) reversibly interconverts 2-phosphoglyceric acid (2-PGA) and phosphoenolpyruvic acid (PEP). The crystal structure of the homodimeric EhENO is presented at a resolution of 1.9 Å. In the crystal structure EhENO presents as an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation. Interestingly, both active sites contain a copurified 2-PGA molecule. While the 2-PGA molecule in the closed active site closely resembles the conformation known from other enolase-2-PGA complexes, the conformation in the open active site is different. Here, 2-PGA is shifted approximately 1.6 Å away from metal ion I, most likely representing a precatalytic situation.

KW - Crystallography, X-Ray

KW - Entamoeba histolytica/enzymology

KW - Humans

KW - Models, Molecular

KW - Phosphopyruvate Hydratase/chemistry

KW - Protein Structure, Quaternary

KW - Protein Structure, Tertiary

U2 - 10.1107/S0907444911016544

DO - 10.1107/S0907444911016544

M3 - SCORING: Journal article

C2 - 21697600

VL - 67

SP - 619

EP - 627

JO - ACTA CRYSTALLOGR D

JF - ACTA CRYSTALLOGR D

SN - 2059-7983

IS - Pt 7

ER -