5lun
From Proteopedia
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==Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - P1 ultra-high resolution crystal form in complex with iron, N-oxalylglycine and arginine== | ==Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - P1 ultra-high resolution crystal form in complex with iron, N-oxalylglycine and arginine== | ||
| - | <StructureSection load='5lun' size='340' side='right' caption='[[5lun]], [[Resolution|resolution]] 1.08Å' scene=''> | + | <StructureSection load='5lun' size='340' side='right'caption='[[5lun]], [[Resolution|resolution]] 1.08Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5lun]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUN OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5lun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_savastanoi_pv._phaseolicola Pseudomonas savastanoi pv. phaseolicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LUN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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]] 1.08Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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=5lun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lun OCA], [https://pdbe.org/5lun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lun RCSB], [https://www.ebi.ac.uk/pdbsum/5lun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lun ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5lun" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Pseudomonas savastanoi pv. phaseolicola]] |
| - | [[Category: | + | [[Category: McDonough MA]] |
| - | [[Category: | + | [[Category: Schofield CJ]] |
| - | [[Category: | + | [[Category: Zhang Z]] |
| - | + | ||
| - | + | ||
Current revision
Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - P1 ultra-high resolution crystal form in complex with iron, N-oxalylglycine and arginine
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