5hav: Difference between revisions
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''' | ==Sperm whale myoglobin mutant L29H F33Y F43H (F33Y CuBMb) with oxygen bound== | ||
<StructureSection load='5hav' size='340' side='right' caption='[[5hav]], [[Resolution|resolution]] 1.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hav]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HAV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fwx|4fwx]]</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=5hav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hav OCA], [http://pdbe.org/5hav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hav RCSB], [http://www.ebi.ac.uk/pdbsum/5hav PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Heme-copper oxidases (HCOs) catalyze efficient reduction of O2 to water in biological respiration. Despite progress made in studying native enzymes and their models, the roles played by non-covalent interactions in promoting this activity are still not well understood. Herein, we report EPR spectroscopic studies of cryoreduced oxy-F33Y-CuBMb, a functional model of HCOs engineered in myoglobin (Mb). We find that the cryoreduction at 77K of the O2-bound form, trapped in the conformation of the parent oxyferrous form displays a ferric-hydroperoxo EPR signal, in contrast to the cryoreduced oxy-wild type Mb (WTMb), which is unable to deliver a proton and shows a signal from the peroxo-ferric state. Crystallography of oxy-F33Y-CuBMb reveals an extensive hydrogen-bonding network involving water molecules, which is absent from oxy-WTMb. This H-bonding, proton-delivery network is the key structural feature that has transformed the reversible oxygen-binding protein, WTMb, into F33Y-CuBMb, an oxygen-activating enzyme that reduces oxygen to water. These results provide direct evidence of the importance of H-bonding networks involving water in conferring enzymatic activity to a designed metalloenzyme. Incorporating such extended H-bonding networks in the design of other metalloenzymes may allow conferring and fine-tuning their enzymatic activities. | |||
Spectroscopic and crystallographic evidence for the role of a water-containing hydrogen bonding network in oxidase activity of an engineered myoglobin.,Petrik ID, Davydov R, Ross M, Zhao X, Hoffman B, Lu Y J Am Chem Soc. 2015 Dec 30. PMID:26716352<ref>PMID:26716352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5hav" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lu, Y]] | [[Category: Lu, Y]] | ||
[[Category: Petrik, I D]] | |||
[[Category: Oxidase]] | |||
[[Category: Oxidoreductase]] | |||