8X6M

Crystal Structure of Glycerol Dehydrogenase in the Presence of NAD+ and Glycerol

8X6M の概要

• エントリーDOI: 10.2210/pdb8x6m/pdb
• 分子名称: Glycerol dehydrogenase, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: glycerol dehydrogenase, complex, oxidoreductase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81276.16

構造登録者

Park, T.,Kang, J.Y.,Jin, M.,Yang, J.,Kim, H.,Noh, C.,Eom, S.H. (登録日: 2023-11-21, 公開日: 2024-03-27)

主引用文献

Park, T.,Kang, J.Y.,Jin, M.,Yang, J.,Kim, H.,Noh, C.,Jung, C.H.,Eom, S.H.
Structural insights into the octamerization of glycerol dehydrogenase.
Plos One, 19:e0300541-e0300541, 2024

PubMed Abstract: Glycerol dehydrogenase (GDH) catalyzes glycerol oxidation to dihydroxyacetone in a NAD+-dependent manner. As an initiator of the oxidative pathway of glycerol metabolism, a variety of functional and structural studies of GDH have been conducted previously. Structural studies revealed intriguing features of GDH, like the flexible β-hairpin and its significance. Another commonly reported structural feature is the enzyme's octameric oligomerization, though its structural details and functional significance remained unclear. Here, with a newly reported GDH structure, complexed with both NAD+ and glycerol, we analyzed the octamerization of GDH. Structural analyses revealed that octamerization reduces the structural dynamics of the N-domain, which contributes to more consistently maintaining a distance required for catalysis between the cofactor and substrate. This suggests that octamerization may play a key role in increasing the likelihood of the enzyme reaction by maintaining the ligands in an appropriate configuration for catalysis. These findings expand our understanding of the structure of GDH and its relation to the enzyme's activity.

PubMed: 38483875
DOI: 10.1371/journal.pone.0300541

実験手法

X-RAY DIFFRACTION (2 Å)