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Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 angstrom resolution

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Taschner,  Michael
Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society;

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Basquin,  Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Benda,  Christian
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Lorentzen,  Esben
Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society;

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Taschner, M., Basquin, J., Benda, C., & Lorentzen, E. (2013). Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 angstrom resolution. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 81(8), 1473-1478. doi:10.1002/prot.24296.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-1A5A-3
Abstract
Two important steps of the de novo purine biosynthesis pathway are catalyzed by the 5-aminoimidazole ribonucleotide carboxylase and the 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase enzymes. In most eukaryotic organisms, these two activities are present in the bifunctional enzyme complex known as PAICS. We have determined the 2.8-angstrom resolution crystal structure of the 350-kDa invertebrate PAICS from insect cells (Trichoplusia ni) using single-wavelength anomalous dispersion methods. Comparison of insect PAICS to human and prokaryotic homologs provides insights into substrate binding and reveals a highly conserved enzymatic framework across divergent species. Proteins 2013; 81:1473-1478. (c) 2013 Wiley Periodicals, Inc.