5yl3: Difference between revisions

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-'''Unreleased structure'''
-The entry 5yl3 is ON HOLD  until Paper Publication
+==Crystal structure of horse heart myoglobin reconstituted with manganese porphycene in resting state at pH 8.5==
+<StructureSection load='5yl3' size='340' side='right' caption='[[5yl3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5yl3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YL3 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HNN:PORPHYCENE+CONTAINING+MN'>HNN</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yl3 OCA], [http://pdbe.org/5yl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yl3 RCSB], [http://www.ebi.ac.uk/pdbsum/5yl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yl3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A mechanistic study of H2O2-dependent C-H bond hydroxylation by myoglobin reconstituted with a manganese porphycene was carried out. The X-ray crystal structure of the reconstituted protein obtained at 1.5 A resolution reveals tight incorporation of the complex into the myoglobin matrix at pH 8.5, the optimized pH value for the highest turnover number of hydroxylation of ethylbenzene. The protein generates a spectroscopically detectable two-electron oxidative intermediate in a reaction with peracid, which has a half-life up to 38 s at 10 degrees C. Electron paramagnetic resonance spectra of the intermediate with perpendicular and parallel modes are silent, indicating formation of a low-spin Mn(V)-oxo species. In addition, the Mn(V)-oxo species is capable of promoting the hydroxylation of sodium 4-ethylbenzenesulfonate under single turnover conditions with an apparent second-order rate constant of 2.0 M(-1) s(-1) at 25 degrees C. Furthermore, the higher bond dissociation enthalpy of the substrate decreases the rate constant, in support of the proposal that the H-abstraction is one of the rate-limiting steps. The present engineered myoglobin serves as an artificial metalloenzyme for inert C-H bond activation via a high-valent metal species similar to the species employed by native monooxygenases such as cytochrome P450.
-Authors:
+Manganese(V) Porphycene Complex Responsible for Inert C-H Bond Hydroxylation in a Myoglobin Matrix.,Oohora K, Meichin H, Kihira Y, Sugimoto H, Shiro Y, Hayashi T J Am Chem Soc. 2017 Dec 14. doi: 10.1021/jacs.7b11288. PMID:29237270<ref>PMID:29237270</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5yl3" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Equus caballus]]
+[[Category: Hayashi, T]]
+[[Category: Kihira, Y]]
+[[Category: Meichin, H]]
+[[Category: Oohora, K]]
+[[Category: Shiro, Y]]
+[[Category: Sugimoto, H]]
+[[Category: Globin fold]]
+[[Category: Muscle]]
+[[Category: Oxygen storage]]
+[[Category: Oxygen transport]]