Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA

Scott Bailey; Svetlana E. Sedelnikova; G. Michael Blackburn; Hend M. Abdelghany; Alexander G. McLennan; John B. Rafferty

doi:10.1107/S0907444902000768

Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA

Scott Bailey, Svetlana E. Sedelnikova, G. Michael Blackburn, Hend M. Abdelghany, Alexander G. McLennan, John B. Rafferty

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

The molecule diadenosine tetraphosphate (Ap₄A) has been suggested to be a component of the cellular response to metabolic stress and/or, via the intracellular Ap₃A/Ap₄A ratio, to be involved in differentiation and apoptosis. Thus, the enzyme Ap₄A hydrolase has a key metabolic role through regulation of the intracellular Ap₄A levels. Crystals of this enzyme from the nematode Caenorhabditis elegans have been obtained in the presence of a non-hydrolysable substrate analogue, AppCH₂ppA. The crystals belong to space group P2₁, unit-cell parameters a = 57.6, b = 36.8, c = 68.9 Å, β = 114.2°, and diffract to approximately 2.0 Å. Determination of the structure of this complex will provide insights into the substrate specificity and catalytic activity of this class of enzymes.

Original language	English (US)
Pages (from-to)	526-528
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	3
DOIs	https://doi.org/10.1107/S0907444902000768
State	Published - 2002
Externally published	Yes

ASJC Scopus subject areas

Structural Biology

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Bailey, S., Sedelnikova, S. E., Blackburn, G. M., Abdelghany, H. M., McLennan, A. G., & Rafferty, J. B. (2002). Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA. Acta Crystallographica Section D: Biological Crystallography, 58(3), 526-528. https://doi.org/10.1107/S0907444902000768

Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA. / Bailey, Scott; Sedelnikova, Svetlana E.; Blackburn, G. Michael et al.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 3, 2002, p. 526-528.

Research output: Contribution to journal › Article › peer-review

Bailey, S, Sedelnikova, SE, Blackburn, GM, Abdelghany, HM, McLennan, AG & Rafferty, JB 2002, 'Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA', Acta Crystallographica Section D: Biological Crystallography, vol. 58, no. 3, pp. 526-528. https://doi.org/10.1107/S0907444902000768

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title = "Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA",

abstract = "The molecule diadenosine tetraphosphate (Ap4A) has been suggested to be a component of the cellular response to metabolic stress and/or, via the intracellular Ap3A/Ap4A ratio, to be involved in differentiation and apoptosis. Thus, the enzyme Ap4A hydrolase has a key metabolic role through regulation of the intracellular Ap4A levels. Crystals of this enzyme from the nematode Caenorhabditis elegans have been obtained in the presence of a non-hydrolysable substrate analogue, AppCH2ppA. The crystals belong to space group P21, unit-cell parameters a = 57.6, b = 36.8, c = 68.9 {\AA}, β = 114.2°, and diffract to approximately 2.0 {\AA}. Determination of the structure of this complex will provide insights into the substrate specificity and catalytic activity of this class of enzymes.",

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AB - The molecule diadenosine tetraphosphate (Ap4A) has been suggested to be a component of the cellular response to metabolic stress and/or, via the intracellular Ap3A/Ap4A ratio, to be involved in differentiation and apoptosis. Thus, the enzyme Ap4A hydrolase has a key metabolic role through regulation of the intracellular Ap4A levels. Crystals of this enzyme from the nematode Caenorhabditis elegans have been obtained in the presence of a non-hydrolysable substrate analogue, AppCH2ppA. The crystals belong to space group P21, unit-cell parameters a = 57.6, b = 36.8, c = 68.9 Å, β = 114.2°, and diffract to approximately 2.0 Å. Determination of the structure of this complex will provide insights into the substrate specificity and catalytic activity of this class of enzymes.

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Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA

Abstract

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