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5lun

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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

Structural highlights

5lun is a 4 chain structure with sequence from Pseudomonas savastanoi pv. phaseolicola. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.08Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EFE_PSESH Simultaneously catalyzes two reactions, namely formation of ethylene and of succinate from 2-oxoglutarate, with a molar ratio of 2:1.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fukuda H, Ogawa T, Tazaki M, Nagahama K, Fujii T, Tanase S, Morino Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem Biophys Res Commun. 1992 Oct 30;188(2):483-9. PMID:1445291
↑ Zhang Z, Smart TJ, Choi H, Hardy F, Lohans CT, Abboud MI, Richardson MSW, Paton RS, McDonough MA, Schofield CJ. Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate. 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 doi:http://dx.doi.org/10.1073/pnas.1617760114

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lun"

Categories: Large Structures | Pseudomonas savastanoi pv. phaseolicola | McDonough MA | Schofield CJ | Zhang Z

@@ Line 3: / Line 3: @@
 <StructureSection load='5lun' size='340' side='right'caption='[[5lun]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Psesh Psesh]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5LUN FirstGlance]. <br>
+<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" 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efe ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=319 PSESH])</td></tr>
+<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'>[http://proteopedia.org/fgij/fg.htm?mol=5lun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lun OCA], [http://pdbe.org/5lun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lun RCSB], [http://www.ebi.ac.uk/pdbsum/5lun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lun 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=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>
 == 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>
+[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 ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Psesh]]
+[[Category: Pseudomonas savastanoi pv. phaseolicola]]
-[[Category: McDonough, M A]]
+[[Category: McDonough MA]]
-[[Category: Schofield, C J]]
+[[Category: Schofield CJ]]
-[[Category: Zhang, Z]]
+[[Category: Zhang Z]]
-[[Category: 2-oxoglutarate and ferrous iron dependent oxygenase]]
-[[Category: Double stranded beta helix]]
-[[Category: Ethylene forming]]
-[[Category: Oxidoreductase]]

5lun

From Proteopedia

Current revision

Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - P1 ultra-high resolution crystal form in complex with iron, N-oxalylglycine and arginine

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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