2BJK

Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound NAD and citrate.

2BJK の概要

• エントリーDOI: 10.2210/pdb2bjk/pdb
• 関連するPDBエントリー: 2BHP 2BHQ 2BJA
• 分子名称: 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, CITRATE ANION, ... (7 entities in total)
• 機能のキーワード: 1-pyrroline-5-carboxylate, dehyrogenase, oxidoreductase
• 由来する生物種: THERMUS THERMOPHILUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117067.33

構造登録者

Inagaki, E.,Tahirov, T.H. (登録日: 2005-02-04, 公開日: 2006-03-09, 最終更新日: 2025-10-01)

主引用文献

Inagaki, E.,Ohshima, N.,Takahashi, H.,Kuroishi, C.,Yokoyama, S.,Tahirov, T.H.
Crystal Structure of Thermus Thermophilus Delta(1)- Pyrroline-5-Carboxylate Dehydrogenase.
J.Mol.Biol., 362:490-, 2006

PubMed Abstract: Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of Delta(1)-pyrroline-5-carboxylate, into glutamate with the reduction of NAD(+) into NADH. We have confirmed the P5CDh activity of the Thermus thermophilus protein TT0033 (TtP5CDh), and determined the crystal structure of the enzyme in the ligand-free form at 1.4 A resolution. To investigate the structural basis of TtP5CDh function, the TtP5CDh structures with NAD(+), with NADH, and with its product glutamate were determined at 1.8 A, 1.9 A, and 1.4 A resolution, respectively. The solved structures suggest an overall view of the P5CDh catalytic mechanism and provide insights into the P5CDh deficiencies in the case of the human type II hyperprolinemia.

PubMed: 16934832
DOI: 10.1016/J.JMB.2006.07.048

実験手法

X-RAY DIFFRACTION (1.4 Å)