5KJS

Crystal Structure of Arabidopsis thaliana HCT

Summary for 5KJS

• Entry DOI: 10.2210/pdb5kjs/pdb
• Related: 5KJT 5KJU
• Descriptor: Shikimate O-hydroxycinnamoyltransferase (2 entities in total)
• Functional Keywords: phenylpropanoid metabolism, bahd, acyltransferase, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 48619.48

Authors

Levsh, O.,Chiang, Y.C.,Tung, C.,Noel, J.P.,Wang, Y.,Weng, J.K. (deposition date: 2016-06-20, release date: 2016-11-02, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.203 Å)