Crystallization of a complex ofCaenorhabditis elegansdiadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA
| Autor: | Svetlana E. Sedelnikova, Alexander G. McLennan, John B. Rafferty, Hend M. Abdelghany, Scott Bailey, G. Michael Blackburn |
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| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
biology Protein Conformation Substrate (chemistry) General Medicine Crystallography X-Ray biology.organism_classification Acid Anhydride Hydrolases Substrate Specificity chemistry.chemical_compound Enzyme chemistry Biochemistry Structural Biology Apoptosis Hydrolase Animals Molecule Caenorhabditis elegans Crystallization Ap4A Dinucleoside Phosphates Intracellular |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 58:526-528 |
| ISSN: | 0907-4449 |
| Popis: | The molecule diadenosine tetraphosphate (Ap(4)A) has been suggested to be a component of the cellular response to metabolic stress and/or, via the intracellular Ap(3)A/Ap(4)A ratio, to be involved in differentiation and apoptosis. Thus, the enzyme Ap(4)A hydrolase has a key metabolic role through regulation of the intracellular Ap(4)A levels. Crystals of this enzyme from the nematode Caenorhabditis elegans have been obtained in the presence of a non-hydrolysable substrate analogue, AppCH(2)ppA. The crystals belong to space group P2(1), unit-cell parameters a = 57.6, b = 36.8, c = 68.9 A, beta = 114.2 degrees, and diffract to approximately 2.0 A. Determination of the structure of this complex will provide insights into the substrate specificity and catalytic activity of this class of enzymes. |
| Databáze: | OpenAIRE |
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