4JA0: Crystal Structure Of The Invertebrate Bi-functional Purine Biosynthesis Enzyme Paics At 2.8 A Resolution

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.
PDB ID: 4JA0Download
MMDB ID: 108019
PDB Deposition Date: 2013/2/18
Updated in MMDB: 2013/10
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4JA0: octameric; determined by author and by software (PISA)
Molecular Components in 4JA0
Label Count Molecule
Proteins (8 molecules)
Phosphoribosylaminoimidazole Carboxylase
Molecule annotation
Chemicals (34 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB