4JA0

Crystal structure of the invertebrate bi-functional purine biosynthesis enzyme PAICS at 2.8 A resolution

4JA0 の概要

• エントリーDOI: 10.2210/pdb4ja0/pdb
• 分子名称: Phosphoribosylaminoimidazole carboxylase, SULFATE ION (3 entities in total)
• 機能のキーワード: saicar pure, purine biosynthesis, protein binding
• 由来する生物種: Bombyx mori (silk moth,silkworm)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 191262.57

構造登録者

Taschner, M.,Basquin, J.,Benda, C.,Lorentzen, E. (登録日: 2013-02-18, 公開日: 2013-02-27, 最終更新日: 2023-09-20)

主引用文献

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

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: 23553965
DOI: 10.1002/prot.24296

実験手法

X-RAY DIFFRACTION (2.8 Å)