2GER

Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase

2GER の概要

• エントリーDOI: 10.2210/pdb2ger/pdb
• 分子名称: Pyrroline-5-carboxylate reductase 1 (2 entities in total)
• 機能のキーワード: oxidative mechanism of human pyrroline-5-carboxylate, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion: P32322
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 168154.46

構造登録者

Meng, Z.,Lou, Z.,Liu, Z.,Rao, Z. (登録日: 2006-03-20, 公開日: 2006-09-19, 最終更新日: 2024-11-20)

主引用文献

Meng, Z.,Lou, Z.,Liu, Z.,Li, M.,Zhao, X.,Bartlam, M.,Rao, Z.
Crystal structure of human pyrroline-5-carboxylate reductase
J.Mol.Biol., 359:1364-1377, 2006

PubMed Abstract: Pyrroline-5-carboxylate reductase (P5CR) is a universal housekeeping enzyme that catalyzes the reduction of Delta(1)-pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as the cofactor. The enzymatic cycle between P5C and proline is very important for the regulation of amino acid metabolism, intracellular redox potential, and apoptosis. Here, we present the 2.8 Angstroms resolution structure of the P5CR apo enzyme, its 3.1 Angstroms resolution ternary complex with NAD(P)H and substrate-analog. The refined structures demonstrate a decameric architecture with five homodimer subunits and ten catalytic sites arranged around a peripheral circular groove. Mutagenesis and kinetic studies reveal the pivotal roles of the dinucleotide-binding Rossmann motif and residue Glu221 in the human enzyme. Human P5CR is thermostable and the crystals were grown at 37 degrees C. The enzyme is implicated in oxidation of the anti-tumor drug thioproline.

PubMed: 16730026
DOI: 10.1016/j.jmb.2006.04.053

実験手法

X-RAY DIFFRACTION (3.1 Å)