5kjw | pdb_00005kjw

Crystal structure of Coleus blumei HCT in complex with 3-hydroxyacetophenone

spinqualitylabelsall models 5kjw, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kjw is a 2 chain structure with sequence from Plectranthus scutellarioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 53C Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E8ZAP2_PLESU Publication Abstract from PubMed 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. Dynamic Conformational States Dictate Selectivity toward the Native Substrate in a Substrate-Permissive Acyltransferase.,Levsh O, Chiang YC, Tung CF, Noel JP, Wang Y, Weng JK Biochemistry. 2016 Nov 2. PMID:27805809 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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