2UUU

alkyldihydroxyacetonephosphate synthase in P212121

2UUU の概要

• エントリーDOI: 10.2210/pdb2uuu/pdb
• 関連するPDBエントリー: 2UUV
• 分子名称: ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, FLAVIN-ADENINE DINUCLEOTIDE, HEXADECAN-1-OL, ... (4 entities in total)
• 機能のキーワード: transferase, lavoprotein, lipid synthesis, peroxisomal disorder
• 由来する生物種: DICTYOSTELIUM DISCOIDEUM (SLIME MOLD)
• 細胞内の位置: Peroxisome: O96759
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 268530.90

構造登録者

Razeto, A.,Mattiroli, F.,Carpanelli, E.,Aliverti, A.,Pandini, V.,Coda, A.,Mattevi, A. (登録日: 2007-03-07, 公開日: 2007-06-26, 最終更新日: 2023-12-13)

主引用文献

Razeto, A.,Mattiroli, F.,Carpanelli, E.,Aliverti, A.,Pandini, V.,Coda, A.,Mattevi, A.
The Crucial Step in Ether Phospholipid Biosynthesis: Structural Basis of a Noncanonical Reaction Associated with a Peroxisomal Disorder.
Structure, 15:683-, 2007

PubMed Abstract: Ether phospholipids are essential constituents of eukaryotic cell membranes. Rhizomelic chondrodysplasia punctata type 3 is a severe peroxisomal disorder caused by inborn deficiency of alkyldihydroxyacetonephosphate synthase (ADPS). The enzyme carries out the most characteristic step in ether phospholipid biosynthesis: formation of the ether bond. The crystal structure of ADPS from Dictyostelium discoideum shows a fatty-alcohol molecule bound in a narrow hydrophobic tunnel, specific for aliphatic chains of 16 carbons. Access to the tunnel is controlled by a flexible loop and a gating helix at the protein-membrane interface. Structural and mutagenesis investigations identify a cluster of hydrophilic catalytic residues, including an essential tyrosine, possibly involved in substrate proton abstraction, and the arginine that is mutated in ADPS-deficient patients. We propose that ether bond formation might be orchestrated through a covalent imine intermediate with the flavin, accounting for the noncanonical employment of a flavin cofactor in a nonredox reaction.

PubMed: 17562315
DOI: 10.1016/J.STR.2007.04.009

実験手法

X-RAY DIFFRACTION (1.95 Å)