4XAE

Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana

4XAE の概要

• エントリーDOI: 10.2210/pdb4xae/pdb
• 分子名称: Feruloyl CoA ortho-hydroxylase 1, SODIUM ION (3 entities in total)
• 機能のキーワード: protein engineering, coumarins, 2-oxoglutarate dependent dioxygenase, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84659.86

構造登録者

Zhou, D.,Kandavelu, P.,Zhang, H.,Wang, B.C.,Rose, J.,Yan, Y. (登録日: 2014-12-14, 公開日: 2015-06-10, 最終更新日: 2024-11-20)

主引用文献

Sun, X.,Zhou, D.,Kandavelu, P.,Zhang, H.,Yuan, Q.,Wang, B.C.,Rose, J.,Yan, Y.
Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana.
Sci Rep, 5:10355-10355, 2015

PubMed Abstract: Coumarins belong to an important class of plant secondary metabolites. Feruloyl-CoA 6'-hydroxylase (F6'H), a 2-oxoglutarate dependent dioxygenase (2OGD), catalyzes a pivotal step in the biosynthesis of a simple coumarin scopoletin. In this study, we determined the 3-dimensional structure of the F6'H1 apo enzyme by X-ray crystallography. It is the first reported structure of a 2OGD enzyme involved in coumarin biosynthesis and closely resembles the structure of Arabidopsis thaliana anthocyanidin synthase. To better understand the mechanism of enzyme catalysis and substrate specificity, we also generated a homology model of a related ortho-hydroxylase (C2'H) from sweet potato. By comparing these two structures, we targeted two amino acid residues and verified their roles in substrate binding and specificity by site-directed mutagenesis.

PubMed: 25993561
DOI: 10.1038/srep10355

実験手法

X-RAY DIFFRACTION (2.769 Å)