5UBG

Catalytic core domain of Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni with bound Phosphoribosyl-ATP

5UBG の概要

• エントリーDOI: 10.2210/pdb5ubg/pdb
• 関連するPDBエントリー: 5UB9 5UBH 5UBI
• 分子名称: ATP phosphoribosyltransferase, ZINC ION, PHOSPHORIBOSYL ATP, ... (5 entities in total)
• 機能のキーワード: histidine-biosynthesis, hisg, pr-atp, transferase
• 由来する生物種: Campylobacter jejuni (strain RM1221)
• 細胞内の位置: Cytoplasm : Q5HSJ4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52481.59

構造登録者

Mittelstaedt, G.,Jiao, W.,Livingstone, E.K.,Parker, E.J. (登録日: 2016-12-20, 公開日: 2017-12-20, 最終更新日: 2023-10-04)

主引用文献

Mittelstadt, G.,Jiao, W.,Livingstone, E.K.,Moggre, G.J.,Nazmi, A.R.,Parker, E.J.
A dimeric catalytic core relates the short and long forms of ATP-phosphoribosyltransferase.
Biochem. J., 475:247-260, 2018

PubMed Abstract: Adenosine triphosphate (ATP) phosphoribosyltransferase (ATP-PRT) catalyses the first committed step of histidine biosynthesis in plants and microorganisms. Two forms of ATP-PRT have been reported, which differ in their molecular architecture and mechanism of allosteric regulation. The short-form ATP-PRT is a hetero-octamer, with four HisG chains that comprise only the catalytic domains and four separate chains of HisZ required for allosteric regulation by histidine. The long-form ATP-PRT is homo-hexameric, with each chain comprising two catalytic domains and a covalently linked regulatory domain that binds histidine as an allosteric inhibitor. Here, we describe a truncated long-form ATP-PRT from devoid of its regulatory domain (ATP-PRT). Results showed that ATP-PRT is dimeric, exhibits attenuated catalytic activity, and is insensitive to histidine, indicating that the covalently linked regulatory domain plays a role in both catalysis and regulation. Crystal structures were obtained for ATP-PRT in complex with both substrates, and for the first time, the complete product of the reaction. These structures reveal the key features of the active site and provide insights into how substrates move into position during catalysis.

PubMed: 29208762
DOI: 10.1042/BCJ20170762

実験手法

X-RAY DIFFRACTION (1.9 Å)