1G8F

ATP SULFURYLASE FROM S. CEREVISIAE

1G8F の概要

• エントリーDOI: 10.2210/pdb1g8f/pdb
• 関連するPDBエントリー: 1G8G 1G8H
• 分子名称: SULFATE ADENYLYLTRANSFERASE, CADMIUM ION, CALCIUM ION, ... (9 entities in total)
• 機能のキーワード: alpha-beta protein, beta-barrel, rossmann-fold, kinase fold, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P08536
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59548.65

構造登録者

Ullrich, T.C.,Blaesse, M.,Huber, R. (登録日: 2000-11-17, 公開日: 2001-05-23, 最終更新日: 2024-02-07)

主引用文献

Ullrich, T.C.,Blaesse, M.,Huber, R.
Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation.
EMBO J., 20:316-329, 2001

PubMed Abstract: ATP sulfurylases (ATPSs) are ubiquitous enzymes that catalyse the primary step of intracellular sulfate activation: the reaction of inorganic sulfate with ATP to form adenosine-5'-phosphosulfate (APS) and pyrophosphate (PPi). With the crystal structure of ATPS from the yeast Saccharomyces cerevisiae, we have solved the first structure of a member of the ATP sulfurylase family. We have analysed the crystal structure of the native enzyme at 1.95 Angstroms resolution using multiple isomorphous replacement (MIR) and, subsequently, the ternary enzyme product complex with APS and PPi bound to the active site. The enzyme consists of six identical subunits arranged in two stacked rings in a D:3 symmetric assembly. Nucleotide binding causes significant conformational changes, which lead to a rigid body structural displacement of domains III and IV of the ATPS monomer. Despite having similar folds and active site design, examination of the active site of ATPS and comparison with known structures of related nucleotidylyl transferases reveal a novel ATP binding mode that is peculiar to ATP sulfurylases.

PubMed: 11157739
DOI: 10.1093/emboj/20.3.316

実験手法

X-RAY DIFFRACTION (1.95 Å)