4xae

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

Structural highlights

4xae is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.769Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F6H1_ARATH 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)involved in scopoletin biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA but has no activity with ferulic acid, feruloylquinic acid, caffeic acid, caffeoyl CoA, p-coumaric acid, cinnamic acid, cinnamoyl CoA or benzoyl CoA.^[1]

Publication Abstract from PubMed

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.

Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana.,Sun X, Zhou D, Kandavelu P, Zhang H, Yuan Q, Wang BC, Rose J, Yan Y Sci Rep. 2015 May 20;5:10355. doi: 10.1038/srep10355. PMID:25993561^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kai K, Mizutani M, Kawamura N, Yamamoto R, Tamai M, Yamaguchi H, Sakata K, Shimizu B. Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana. Plant J. 2008 Sep;55(6):989-99. doi: 10.1111/j.1365-313X.2008.03568.x. Epub 2008 , Jun 10. PMID:18547395 doi:http://dx.doi.org/10.1111/j.1365-313X.2008.03568.x
↑ Sun X, Zhou D, Kandavelu P, Zhang H, Yuan Q, Wang BC, Rose J, Yan Y. Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana. Sci Rep. 2015 May 20;5:10355. doi: 10.1038/srep10355. PMID:25993561 doi:http://dx.doi.org/10.1038/srep10355

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OCA

[1] Kai K, Mizutani M, Kawamura N, Yamamoto R, Tamai M, Yamaguchi H, Sakata K, Shimizu B. Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana. Plant J. 2008 Sep;55(6):989-99. doi: 10.1111/j.1365-313X.2008.03568.x. Epub 2008 , Jun 10. PMID:18547395 doi:http://dx.doi.org/10.1111/j.1365-313X.2008.03568.x

[2] Sun X, Zhou D, Kandavelu P, Zhang H, Yuan Q, Wang BC, Rose J, Yan Y. Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana. Sci Rep. 2015 May 20;5:10355. doi: 10.1038/srep10355. PMID:25993561 doi:http://dx.doi.org/10.1038/srep10355

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