View source for 3nx2


==Enterobacter sp. Px6-4 Ferulic Acid Decarboxylase in complex with substrate analogues==
<StructureSection load='3nx2' size='340' side='right'caption='[[3nx2]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nx2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp._Px6-4 Enterobacter sp. Px6-4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NX2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FER:3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC+ACID'>FER</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=3nx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nx2 OCA], [https://pdbe.org/3nx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nx2 RCSB], [https://www.ebi.ac.uk/pdbsum/3nx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nx2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C6F3U5_9ENTR C6F3U5_9ENTR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microbial ferulic acid decarboxylase (FADase) catalyzes the transformation of ferulic acid to 4-hydroxy-3-methoxystyrene (4-vinylguaiacol) via non-oxidative decarboxylation. Here we report the crystal structures of the Enterobacter sp. Px6-4 FADase and the enzyme in complex with substrate analogues. Our analyses revealed that FADase possessed a half-opened bottom beta-barrel with the catalytic pocket located between the middle of the core beta-barrel and the helical bottom. Its structure shared a high degree of similarity with members of the phenolic acid decarboxylase (PAD) superfamily. Structural analysis revealed that FADase catalyzed reactions by an "open-closed" mechanism involving a pocket of 8x8x15 A dimension on the surface of the enzyme. The active pocket could directly contact the solvent and allow the substrate to enter when induced by substrate analogues. Site-directed mutagenesis showed that the E134A mutation decreased the enzyme activity by more than 60%, and Y21A and Y27A mutations abolished the enzyme activity completely. The combined structural and mutagenesis results suggest that during decarboxylation of ferulic acid by FADase, Trp25 and Tyr27 are required for the entering and proper orientation of the substrate while Glu134 and Asn23 participate in proton transfer.

Structural Basis of Enzymatic Activity for the Ferulic Acid Decarboxylase (FADase) from Enterobacter sp. Px6-4.,Gu W, Yang J, Lou Z, Liang L, Sun Y, Huang J, Li X, Cao Y, Meng Z, Zhang KQ PLoS One. 2011 Jan 21;6(1):e16262. PMID:21283705<ref>PMID:21283705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3nx2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterobacter sp. Px6-4]]
[[Category: Large Structures]]
[[Category: Gu W]]
[[Category: Lou ZY]]
[[Category: Meng ZH]]
[[Category: Yang JK]]
[[Category: Zhang K-Q]]