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5kjv

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjv OCA], [http://pdbe.org/5kjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjv RCSB], [http://www.ebi.ac.uk/pdbsum/5kjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjv OCA], [http://pdbe.org/5kjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjv RCSB], [http://www.ebi.ac.uk/pdbsum/5kjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:27805809</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kjv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 03:38, 10 December 2016

Crystal structure of Coleus blumei HCT

5kjv, resolution 1.75Å

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