4JA0
Crystal structure of the invertebrate bi-functional purine biosynthesis enzyme PAICS at 2.8 A resolution
Summary for 4JA0
| Entry DOI | 10.2210/pdb4ja0/pdb |
| Descriptor | Phosphoribosylaminoimidazole carboxylase, SULFATE ION (3 entities in total) |
| Functional Keywords | saicar pure, purine biosynthesis, protein binding |
| Biological source | Bombyx mori (silk moth,silkworm) |
| Total number of polymer chains | 4 |
| Total formula weight | 191262.57 |
| Authors | Taschner, M.,Basquin, J.,Benda, C.,Lorentzen, E. (deposition date: 2013-02-18, release date: 2013-02-27, Last modification date: 2023-09-20) |
| Primary citation | Taschner, M.,Basquin, J.,Benda, C.,Lorentzen, E. Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 angstrom resolution. Proteins, 81:1473-1478, 2013 Cited by PubMed 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-Å 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. PubMed: 23553965DOI: 10.1002/prot.24296 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
