1GPH

STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS

1GPH の概要

• エントリーDOI: 10.2210/pdb1gph/pdb
• 分子名称: GLUTAMINE PHOSPHORIBOSYL-PYROPHOSPHATE AMIDOTRANSFERASE, IRON/SULFUR CLUSTER, ADENOSINE MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase, glutamine amidotransferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 206213.14

構造登録者

Smith, J.L. (登録日: 1994-04-20, 公開日: 1994-07-31, 最終更新日: 2024-02-07)

主引用文献

Smith, J.L.,Zaluzec, E.J.,Wery, J.P.,Niu, L.,Switzer, R.L.,Zalkin, H.,Satow, Y.
Structure of the allosteric regulatory enzyme of purine biosynthesis.
Science, 264:1427-1433, 1994

PubMed Abstract: Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate (PRPP) amidotransferase, from Bacillus subtilis. This allosteric enzyme, a 200-kilodalton tetramer, is subject to end product regulation by purine nucleotides. The metalloenzyme from B. subtilis is a paradigm for the higher eukaryotic enzymes, which have been refractory to isolation in stable form. The two folding domains of the polypeptide are correlated with functional domains for glutamine binding and for transfer of ammonia to the substrate PRPP. Eight molecules of the feedback inhibitor adenosine monophosphate (AMP) are bound to the tetrameric enzyme in two types of binding sites: the PRPP catalytic site of each subunit and an unusual regulatory site that is immediately adjacent to each active site but is between subunits. An oxygen-sensitive [4Fe-4S] cluster in each subunit is proposed to regulate protein turnover in vivo and is distant from the catalytic site. Oxygen sensitivity of the cluster is diminished by AMP, which blocks a channel through the protein to the cluster. The structure is representative of both glutamine amidotransferases and phosphoribosyltransferases.

PubMed: 8197456

実験手法

X-RAY DIFFRACTION (3 Å)