Structural highlights
Function
Q1HQ66_BOMMO
Publication Abstract from PubMed
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-A 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.
Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 A resolution.,Taschner M, Basquin J, Benda C, Lorentzen E Proteins. 2013 Aug;81(8):1473-8. doi: 10.1002/prot.24296. Epub 2013 Jun 1. PMID:23553965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Taschner M, Basquin J, Benda C, Lorentzen E. Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 A resolution. Proteins. 2013 Aug;81(8):1473-8. doi: 10.1002/prot.24296. Epub 2013 Jun 1. PMID:23553965 doi:http://dx.doi.org/10.1002/prot.24296