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, Vol. 67, No. Pt 7, 07.2011, p. 619-27.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -