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Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 01; 65(Pt 11):1153-6.AC

Abstract

Escherichia coli isocitrate dehydrogenase (ICDH) can be phosphorylated and dephosphorylated by a single bifunctional protein, isocitrate dehydrogenase kinase/phosphatase (AceK), which is encoded by the aceK gene. In order to investigate the regulatory mechanism of (de)phosphorylation of ICDH by AceK, AceK was successfully cocrystallized in complex with its intact protein substrate, ICDH, in the presence of ATP. The complex crystal was obtained by the hanging-drop vapour-diffusion technique using PEG 300 as a precipitant and magnesium sulfate as an additive. SDS-PAGE analysis of dissolved crystals showed that the crystals contained both AceK and ICDH proteins. The complex crystals diffracted to a resolution of 2.9 angstrom in space group P6(3), with unit-cell parameters a = b = 196.80, c = 156.46 angstrom.

Authors+Show Affiliations

Department of Biochemistry, Queen's University, Kingston, ON, Canada.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19923739

Citation

Zheng, Jimin, et al. "Purification, Crystallization and Preliminary X-ray Analysis of Bifunctional Isocitrate Dehydrogenase Kinase/phosphatase in Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 65, no. Pt 11, 2009, pp. 1153-6.
Zheng J, Ji AX, Jia Z. Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009;65(Pt 11):1153-6.
Zheng, J., Ji, A. X., & Jia, Z. (2009). Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 65(Pt 11), 1153-6. https://doi.org/10.1107/S1744309109038718
Zheng J, Ji AX, Jia Z. Purification, Crystallization and Preliminary X-ray Analysis of Bifunctional Isocitrate Dehydrogenase Kinase/phosphatase in Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1153-6. PubMed PMID: 19923739.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli. AU - Zheng,Jimin, AU - Ji,Alan Xian, AU - Jia,Zongchao, Y1 - 2009/10/30/ PY - 2009/07/23/received PY - 2009/09/24/accepted PY - 2009/11/20/entrez PY - 2009/11/20/pubmed PY - 2010/2/4/medline SP - 1153 EP - 6 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 65 IS - Pt 11 N2 - Escherichia coli isocitrate dehydrogenase (ICDH) can be phosphorylated and dephosphorylated by a single bifunctional protein, isocitrate dehydrogenase kinase/phosphatase (AceK), which is encoded by the aceK gene. In order to investigate the regulatory mechanism of (de)phosphorylation of ICDH by AceK, AceK was successfully cocrystallized in complex with its intact protein substrate, ICDH, in the presence of ATP. The complex crystal was obtained by the hanging-drop vapour-diffusion technique using PEG 300 as a precipitant and magnesium sulfate as an additive. SDS-PAGE analysis of dissolved crystals showed that the crystals contained both AceK and ICDH proteins. The complex crystals diffracted to a resolution of 2.9 angstrom in space group P6(3), with unit-cell parameters a = b = 196.80, c = 156.46 angstrom. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/19923739/Purification_crystallization_and_preliminary_X_ray_analysis_of_bifunctional_isocitrate_dehydrogenase_kinase/phosphatase_in_complex_with_its_substrate_isocitrate_dehydrogenase_from_Escherichia_coli_ L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309109038718 DB - PRIME DP - Unbound Medicine ER -