6PX2

Acropora millepora GAPDH

「6DFZ」から置き換えられました

6PX2 の概要

• エントリーDOI: 10.2210/pdb6px2/pdb
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: complex with nad, oxidoreductase
• 由来する生物種: Acropora millepora (Staghorn coral)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 317675.79

構造登録者

Brandt, G.S.,Fields, P.A. (登録日: 2019-07-24, 公開日: 2019-12-25, 最終更新日: 2024-01-17)

主引用文献

Perez, A.M.,Wolfe, J.A.,Schermerhorn, J.T.,Qian, Y.,Cela, B.A.,Kalinowski, C.R.,Largoza, G.E.,Fields, P.A.,Brandt, G.S.
Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coral Acropora millepora.
Rsc Adv, 11:10364-10374, 2021

PubMed Abstract: Corals are vulnerable to increasing ocean temperatures. It is known that elevated temperatures lead to the breakdown of an essential mutualistic relationship with photosynthetic algae. The molecular mechanisms of this temperature-dependent loss of symbiosis are less well understood. Here, the thermal stability of a critical metabolic enzyme, glyceraldehyde-3-phosphate dehydrogenase, from the stony coral was found to increase significantly in the presence of its cofactor NAD. Determination of the structure of the cofactor-enzyme complex (PDB ID 6PX2) revealed variable NAD occupancy across the four monomers of the tetrameric enzyme. The structure of the fully occupied monomers was compared to those with partial cofactor occupancy, identifying regions of difference that may account for the increased thermal stability.

PubMed: 35423531
DOI: 10.1039/d0ra10119b

実験手法

X-RAY DIFFRACTION (2.4 Å)