English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons78783

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

/persons/resource/persons77713

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

/persons/resource/persons77736

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

/persons/resource/persons78333

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

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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: https://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.