5KJU
Crystal structure of Arabidopsis thaliana HCT in complex with p-coumaroylshikimate
Summary for 5KJU
| Entry DOI | 10.2210/pdb5kju/pdb |
| Related | 5KJS 5KJT |
| Descriptor | Shikimate O-hydroxycinnamoyltransferase, (3~{R},4~{S},5~{R})-3-[(~{E})-3-(4-hydroxyphenyl)prop-2-enoyl]oxy-4,5-bis(oxidanyl)cyclohexene-1-carboxylic acid (3 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 | 48347.02 |
| Authors | Levsh, O.,Chiang, Y.C.,Tung, C.F.,Noel, J.P.,Wang, Y.,Weng, J.K. (deposition date: 2016-06-20, release date: 2016-11-02, Last modification date: 2024-03-06) |
| 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 Cited by 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: 27805809DOI: 10.1021/acs.biochem.6b00887 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.44 Å) |
Structure validation
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