5WRI

Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and C4 peptide

5WRI の概要

• エントリーDOI: 10.2210/pdb5wri/pdb
• 関連するPDBエントリー: 3AP1 5WRJ
• 分子名称: Protein-tyrosine sulfotransferase 1, ASP-PHE-GLU-ASP-TYR-GLU-PHE-ASP, ADENOSINE-3'-5'-DIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Golgi apparatus membrane ; Single-pass type II membrane protein : O60507
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75743.27

構造登録者

Tanaka, S.,Nishiyori, T.,Kojo, H.,Otsubo, R.,Kakuta, Y. (登録日: 2016-12-02, 公開日: 2017-09-13)

主引用文献

Tanaka, S.,Nishiyori, T.,Kojo, H.,Otsubo, R.,Tsuruta, M.,Kurogi, K.,Liu, M.C.,Suiko, M.,Sakakibara, Y.,Kakuta, Y.
Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1.
Sci Rep, 7:8776-8776, 2017

PubMed Abstract: Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.

PubMed: 28821720
DOI: 10.1038/s41598-017-07141-8

実験手法

X-RAY DIFFRACTION (1.6 Å)