4XAE

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

Summary for 4XAE

• Entry DOI: 10.2210/pdb4xae/pdb
• Descriptor: Feruloyl CoA ortho-hydroxylase 1, SODIUM ION (3 entities in total)
• Functional Keywords: protein engineering, coumarins, 2-oxoglutarate dependent dioxygenase, oxidoreductase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 84659.86

Authors

Zhou, D.,Kandavelu, P.,Zhang, H.,Wang, B.C.,Rose, J.,Yan, Y. (deposition date: 2014-12-14, release date: 2015-06-10, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.769 Å)