3U3K

Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol

3U3K の概要

• エントリーDOI: 10.2210/pdb3u3k/pdb
• 関連するPDBエントリー: 3U3J 3U3M 3U3O 3U3R
• 分子名称: Sulfotransferase 1A1, ADENOSINE-3'-5'-DIPHOSPHATE, naphthalen-2-ol, ... (4 entities in total)
• 機能のキーワード: arylsulfotransferase, binding sites, 2-naphtol, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P50225
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73926.07

構造登録者

Guttman, C.,Berger, I.,Aharoni, A.,Zarivach, R. (登録日: 2011-10-06, 公開日: 2011-11-16, 最終更新日: 2023-09-13)

主引用文献

Berger, I.,Guttman, C.,Amar, D.,Zarivach, R.,Aharoni, A.
The molecular basis for the broad substrate specificity of human sulfotransferase 1A1.
Plos One, 6:e26794-e26794, 2011

PubMed Abstract: Cytosolic sulfotransferases (SULTs) are mammalian enzymes that detoxify a wide variety of chemicals through the addition of a sulfate group. Despite extensive research, the molecular basis for the broad specificity of SULTs is still not understood. Here, structural, protein engineering and kinetic approaches were employed to obtain deep understanding of the molecular basis for the broad specificity, catalytic activity and substrate inhibition of SULT1A1. We have determined five new structures of SULT1A1 in complex with different acceptors, and utilized a directed evolution approach to generate SULT1A1 mutants with enhanced thermostability and increased catalytic activity. We found that active site plasticity enables binding of different acceptors and identified dramatic structural changes in the SULT1A1 active site leading to the binding of a second acceptor molecule in a conserved yet non-productive manner. Our combined approach highlights the dominant role of SULT1A1 structural flexibility in controlling the specificity and activity of this enzyme.

PubMed: 22069470
DOI: 10.1371/journal.pone.0026794

実験手法

X-RAY DIFFRACTION (2.36 Å)