5kjs: Difference between revisions
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==Crystal Structure of Arabidopsis thaliana HCT== | ==Crystal Structure of Arabidopsis thaliana HCT== | ||
<StructureSection load='5kjs' size='340' side='right' caption='[[5kjs]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5kjs' size='340' side='right'caption='[[5kjs]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kjs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJS FirstGlance]. <br> | <table><tr><td colspan='2'>[[5kjs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJS FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | [[Category: Arath]] | ||
[[Category: Large Structures]] | |||
[[Category: Shikimate O-hydroxycinnamoyltransferase]] | [[Category: Shikimate O-hydroxycinnamoyltransferase]] | ||
[[Category: Chiang, Y C]] | [[Category: Chiang, Y C]] | ||
Revision as of 19:26, 20 November 2019
Crystal Structure of Arabidopsis thaliana HCTCrystal Structure of Arabidopsis thaliana HCT
Structural highlights
Function[HST_ARATH] Acyltransferase involved in the biosynthesis of lignin. Accepts caffeoyl-CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on both shikimate and quinate acceptors.[1] Publication Abstract from PubMedHydroxycinnamoyl-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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