4MND

Crystal structure of Archaeoglobus fulgidus IPCT-DIPPS bifunctional membrane protein

4MND の概要

• エントリーDOI: 10.2210/pdb4mnd/pdb
• 分子名称: CTP L-myo-inositol-1-phosphate cytidylyltransferase/CDP-L-myo-inositol myo-inositolphosphotransferase, EICOSANE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: transmembrane protein, rossmann fold, cdp-alcohol phosphotransferase, transferase
• 由来する生物種: Archaeoglobus fulgidus
• 細胞内の位置: Membrane; Multi-pass membrane protein (Potential): O29976
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54786.91

構造登録者

Nogly, P.,Gushchin, I.,Remeeva, A.,Esteves, A.M.,Ishchenko, A.,Ma, P.,Grudinin, S.,Borges, N.,Round, E.,Moraes, I.,Borshchevskiy, V.,Santos, H.,Gordeliy, V.,Archer, M. (登録日: 2013-09-10, 公開日: 2014-07-02, 最終更新日: 2023-09-20)

主引用文献

Nogly, P.,Gushchin, I.,Remeeva, A.,Esteves, A.M.,Borges, N.,Ma, P.,Ishchenko, A.,Grudinin, S.,Round, E.,Moraes, I.,Borshchevskiy, V.,Santos, H.,Gordeliy, V.,Archer, M.
X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism.
Nat Commun, 5:4169-4169, 2014

PubMed Abstract: Phospholipids have major roles in the structure and function of all cell membranes. Most integral membrane proteins from the large CDP-alcohol phosphatidyltransferase family are involved in phospholipid biosynthesis across the three domains of life. They share a conserved sequence pattern and catalyse the displacement of CMP from a CDP-alcohol by a second alcohol. Here we report the crystal structure of a bifunctional enzyme comprising a cytoplasmic nucleotidyltransferase domain (IPCT) fused with a membrane CDP-alcohol phosphotransferase domain (DIPPS) at 2.65 Å resolution. The bifunctional protein dimerizes through the DIPPS domains, each comprising six transmembrane α-helices. The active site cavity is hydrophilic and widely open to the cytoplasm with a magnesium ion surrounded by four highly conserved aspartate residues from helices TM2 and TM3. We show that magnesium is essential for the enzymatic activity and is involved in catalysis. Substrates docking is validated by mutagenesis studies, and a structure-based catalytic mechanism is proposed.

PubMed: 24942835
DOI: 10.1038/ncomms5169

実験手法

X-RAY DIFFRACTION (2.66 Å)