1FJ2

Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution

1FJ2 の概要

• エントリーDOI: 10.2210/pdb1fj2/pdb
• 関連するPDBエントリー: 1auo
• 分子名称: PROTEIN (ACYL PROTEIN THIOESTERASE 1), BROMIDE ION (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase, serine hydrolase, sad, anomalous diffraction, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : O75608
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53037.68

構造登録者

Devedjiev, Y.,Dauter, Z.,Kuznetsov, S.,Jones, T.,Derewenda, Z. (登録日: 2000-08-07, 公開日: 2000-11-29, 最終更新日: 2024-02-07)

主引用文献

Devedjiev, Y.,Dauter, Z.,Kuznetsov, S.R.,Jones, T.L.,Derewenda, Z.S.
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
Structure Fold.Des., 8:1137-1146, 2000

PubMed Abstract: Many proteins undergo posttranslational modifications involving covalent attachment of lipid groups. Among them is palmitoylation, a dynamic, reversible process that affects trimeric G proteins and Ras and constitutes a regulatory mechanism for signal transduction pathways. Recently, an acylhydrolase previously identified as lysophospholipase has been shown to function as an acyl protein thioesterase, which catalyzes depalmitoylation of Galpha proteins as well as Ras. Its amino acid sequence suggested that the protein is evolutionarily related to neutral lipases and other thioesterases, but direct structural information was not available.

PubMed: 11080636
DOI: 10.1016/S0969-2126(00)00529-3

実験手法

X-RAY DIFFRACTION (1.5 Å)