1J70

CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE

1J70 の概要

• エントリーDOI: 10.2210/pdb1j70/pdb
• 分子名称: ATP SULPHURYLASE, PHOSPHATE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: nucleotide binding fold and 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: 3
• 化学式量合計: 174577.43

構造登録者

Lalor, D.J.,Schnyder, T.,Saridakis, V.,Pilloff, D.E.,Dong, A.,Tang, H.,Leyh, T.S.,Pai, E.F. (登録日: 2001-05-15, 公開日: 2003-06-17, 最終更新日: 2024-02-07)

主引用文献

Lalor, D.J.,Schnyder, T.,Saridakis, V.,Pilloff, D.E.,Dong, A.,Tang, H.,Leyh, T.S.,Pai, E.F.
Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity.
Protein Eng., 16:1071-1079, 2003

PubMed Abstract: ATP sulfurylase catalyzes the first step in the activation of sulfate by transferring the adenylyl-moiety (AMP approximately ) of ATP to sulfate to form adenosine 5'-phosphosulfate (APS) and pyrophosphate (PP(i)). Subsequently, APS kinase mediates transfer of the gamma-phosphoryl group of ATP to APS to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS) and ADP. The recently determined crystal structure of yeast ATP sulfurylase suggests that its C-terminal domain is structurally quite independent from the other domains, and not essential for catalytic activity. It seems, however, to dictate the oligomerization state of the protein. Here we show that truncation of this domain results in a monomeric enzyme with slightly enhanced catalytic efficiency. Structural alignment of the C-terminal domain indicated that it is extremely similar in its fold to APS kinase although not catalytically competent. While carrying out these structural and functional studies a surface groove was noted. Careful inspection and modeling revealed that the groove is sufficiently deep and wide, as well as properly positioned, to act as a substrate channel between the ATP sulfurylase and APS kinase-like domains of the enzyme.

PubMed: 14983089
DOI: 10.1093/protein/gzg133

実験手法

X-RAY DIFFRACTION (2.3 Å)