4N5N

Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha in complexed with NADP

4N5N の概要

• エントリーDOI: 10.2210/pdb4n5n/pdb
• 関連するPDBエントリー: 1q7b 3vzp 4N5L 4N5M
• 分子名称: Acetoacetyl-CoA reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha/beta structure, oxidoreductase
• 由来する生物種: Ralstonia eutropha
• 細胞内の位置: Cytoplasm: P14697
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60285.13

構造登録者

Kim, J.-E.,Kim, S.,Kim, K.-J. (登録日: 2013-10-10, 公開日: 2013-12-11, 最終更新日: 2023-11-08)

主引用文献

Kim, J.-E.,Chang, J.H.,Kim, E.-J.,Kim, K.-J.
Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha
Biochem.Biophys.Res.Commun., 443:783-788, 2014

PubMed Abstract: (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha H16 (RePhaB) is an enzyme that catalyzes the NADPH-dependent reduction of acetoacetyl-CoA, an intermediate of polyhydroxyalkanoates (PHA) synthetic pathways. Polymeric PHA is used to make bioplastics, implant biomaterials, and biofuels. Here, we report the crystal structures of RePhaB apoenzyme and in complex with either NADP(+) or acetoacetyl-CoA, which provide the catalytic mechanism of the protein. RePhaB contains a Rossmann fold and a Clamp domain for binding of NADP(+) and acetoacetyl-CoA, respectively. The NADP(+)-bound form of RePhaB structure reveals that the protein has a unique cofactor binding mode. Interestingly, in the RePhaB structure in complex with acetoacetyl-CoA, the conformation of the Clamp domain, especially the Clamp-lid, undergoes a large structural change about 4.6 Å leading to formation of the substrate pocket. These structural observations, along with the biochemical experiments, suggest that movement of the Clamp-lid enables the substrate binding and ensures the acetoacetyl moiety is located near to the nicotinamide ring of NADP(+).

PubMed: 24211201
DOI: 10.1016/j.bbrc.2013.10.150

実験手法

X-RAY DIFFRACTION (1.9 Å)