6BMS

Palmitoyltransferase structure

6BMS の概要

• エントリーDOI: 10.2210/pdb6bms/pdb
• 分子名称: Palmitoyltransferase, ZINC ION, DODECYL-BETA-D-MALTOSIDE, ... (7 entities in total)
• 機能のキーワード: membrane bound enzyme, membrane protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83740.35

構造登録者

Kumar, P.,Rajashankar, K. (登録日: 2017-11-15, 公開日: 2018-01-10, 最終更新日: 2024-03-13)

主引用文献

Rana, M.S.,Kumar, P.,Lee, C.J.,Verardi, R.,Rajashankar, K.R.,Banerjee, A.
Fatty acyl recognition and transfer by an integral membraneS-acyltransferase.
Science, 359:-, 2018

PubMed Abstract: DHHC (Asp-His-His-Cys) palmitoyltransferases are eukaryotic integral membrane enzymes that catalyze protein palmitoylation, which is important in a range of physiological processes, including small guanosine triphosphatase (GTPase) signaling, cell adhesion, and neuronal receptor scaffolding. We present crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface, which allows the enzyme to catalyze thioester-exchange chemistry by using fatty acyl-coenzyme A and explains why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. We propose a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity mutants with preferences for shorter and longer acyl chains.

PubMed: 29326245
DOI: 10.1126/science.aao6326

実験手法

X-RAY DIFFRACTION (2.441 Å)