4uu2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp. Enterobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UU2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4uu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp. Enterobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UU2 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uu2 OCA], [https://pdbe.org/4uu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uu2 RCSB], [https://www.ebi.ac.uk/pdbsum/4uu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uu2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uu2 OCA], [https://pdbe.org/4uu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uu2 RCSB], [https://www.ebi.ac.uk/pdbsum/4uu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uu2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/C6F3U5_9ENTR C6F3U5_9ENTR] | [https://www.uniprot.org/uniprot/C6F3U5_9ENTR C6F3U5_9ENTR] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We report on a 'green' method for the utilization of carbon dioxide as C1 unit for the regioselective synthesis of (E)-cinnamic acids via regioselective enzymatic carboxylation of para-hydroxystyrenes. Phenolic acid decarboxylases from bacterial sources catalyzed the beta-carboxylation of para-hydroxystyrene derivatives with excellent regio- and (E/Z)-stereoselectivity by exclusively acting at the beta-carbon atom of the C=C side chain to furnish the corresponding (E)-cinnamic acid derivatives in up to 40% conversion at the expense of bicarbonate as carbon dioxide source. Studies on the substrate scope of this strategy are presented and a catalytic mechanism is proposed based on molecular modelling studies supported by mutagenesis of amino acid residues in the active site. | ||
| - | |||
| - | Regioselective Enzymatic beta-Carboxylation of -Hydroxy- styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases.,Wuensch C, Pavkov-Keller T, Steinkellner G, Gross J, Fuchs M, Hromic A, Lyskowski A, Fauland K, Gruber K, Glueck SM, Faber K Adv Synth Catal. 2015 May 26;357(8):1909-1918. Epub 2015 Apr 2. PMID:26190963<ref>PMID:26190963</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4uu2" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Ferulic acid decarboxylase from Enterobacter sp., single mutant
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Categories: Enterobacter sp | Large Structures | Faber K | Fauland K | Fuchs M | Glueck SM | Gross J | Gruber K | Hromic A | Lyskowski A | Pavkov-Keller T | Steinkellner G | Wuensch C
