Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli
| Autor: | Ann Lewendon, Tina Izard, John Barker, Arie Geerlof |
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| Rok vydání: | 1999 |
| Předmět: |
Stereochemistry
Protein Conformation Coenzyme A Resolution (electron density) General Medicine medicine.disease_cause Crystallography X-Ray Nucleotidyltransferases chemistry.chemical_compound chemistry Biosynthesis Structural Biology medicine Escherichia coli Phosphopantetheine adenylyltransferase Molecule |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 55(Pt 6) |
| ISSN: | 0907-4449 |
| Popis: | Phosphopantetheine adenylyltransferase (PPAT, E.C. 2.7.7.3) catalyzes the penultimate step in coenzyme A (CoA) biosynthesis, transferring an adenylyl group from ATP to 4′-phosphopantetheine, and forming dephospho-CoA. Cubic crystals of native PPAT from Escherichia coli as well as PPAT in complex with its substrates were obtained. The crystals belong to space group I23 or I213 with unit-cell dimension a = 135.5 Å. The crystals diffract to better than 1.8 Å resolution on a Cu Kα rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 2.9 Å3 Da−1. |
| Databáze: | OpenAIRE |
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