5KJT

Crystal structure of Arabidopsis thaliana HCT in complex with p-coumaroyl-CoA

5KJT の概要

• エントリーDOI: 10.2210/pdb5kjt/pdb
• 関連するPDBエントリー: 5KJS 5KJU
• 分子名称: Shikimate O-hydroxycinnamoyltransferase, p-coumaroyl-CoA (3 entities in total)
• 機能のキーワード: phenylpropanoid metabolism, hct, bahd, acyltransferase, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48940.40

構造登録者

Levsh, O.,Chiang, Y.C.,Tung, C.F.,Noel, J.P.,Wang, Y.,Weng, J.K. (登録日: 2016-06-20, 公開日: 2016-11-02, 最終更新日: 2024-03-06)

主引用文献

Levsh, O.,Chiang, Y.C.,Tung, C.F.,Noel, J.P.,Wang, Y.,Weng, J.K.
Dynamic Conformational States Dictate Selectivity toward the Native Substrate in a Substrate-Permissive Acyltransferase.
Biochemistry, 55:6314-6326, 2016

PubMed Abstract: Hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyltransferase (HCT) is an essential acyltransferase that mediates flux through plant phenylpropanoid metabolism by catalyzing a reaction between p-coumaroyl-CoA and shikimate, yet it also exhibits broad substrate permissiveness in vitro. How do enzymes like HCT avoid functional derailment by cellular metabolites that qualify as non-native substrates? Here, we combine X-ray crystallography and molecular dynamics to reveal distinct dynamic modes of HCT under native and non-native catalysis. We find that essential electrostatic and hydrogen-bonding interactions between the ligand and active site residues, permitted by active site plasticity, are elicited more effectively by shikimate than by other non-native substrates. This work provides a structural basis for how dynamic conformational states of HCT favor native over non-native catalysis by reducing the number of futile encounters between the enzyme and shikimate.

PubMed: 27805809
DOI: 10.1021/acs.biochem.6b00887

実験手法

X-RAY DIFFRACTION (2.5 Å)