View source for 5lsq


==Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - I222 crystal form==
<StructureSection load='5lsq' size='340' side='right'caption='[[5lsq]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lsq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LSQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsq OCA], [http://pdbe.org/5lsq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lsq RCSB], [http://www.ebi.ac.uk/pdbsum/5lsq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsq ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/EFE_PSESH EFE_PSESH]] Simultaneously catalyzes two reactions, namely formation of ethylene and of succinate from 2-oxoglutarate, with a molar ratio of 2:1.<ref>PMID:1445291</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ethylene is important in industry and biological signaling. In plants, ethylene is produced by oxidation of 1-aminocyclopropane-1-carboxylic acid, as catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase. Bacteria catalyze ethylene production, but via the four-electron oxidation of 2-oxoglutarate to give ethylene in an arginine-dependent reaction. Crystallographic and biochemical studies on the Pseudomonas syringae ethylene-forming enzyme reveal a branched mechanism. In one branch, an apparently typical 2-oxoglutarate oxygenase reaction to give succinate, carbon dioxide, and sometimes pyrroline-5-carboxylate occurs. Alternatively, Grob-type oxidative fragmentation of a 2-oxoglutarate-derived intermediate occurs to give ethylene and carbon dioxide. Crystallographic and quantum chemical studies reveal that fragmentation to give ethylene is promoted by binding of l-arginine in a nonoxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene, relative to succinate formation.

Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.,Zhang Z, Smart TJ, Choi H, Hardy F, Lohans CT, Abboud MI, Richardson MSW, Paton RS, McDonough MA, Schofield CJ Proc Natl Acad Sci U S A. 2017 May 2;114(18):4667-4672. doi:, 10.1073/pnas.1617760114. Epub 2017 Apr 18. PMID:28420789<ref>PMID:28420789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lsq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 19310]]
[[Category: Large Structures]]
[[Category: McDonough, M A]]
[[Category: Schofield, C J]]
[[Category: Zhang, Z]]
[[Category: 2-oxoglutarate and ferrous iron dependent oxygenase]]
[[Category: Double stranded beta helix]]
[[Category: Ethylene forming]]
[[Category: Oxidoreductase]]