5oja

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m (Protected "5oja" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5oja is ON HOLD until Paper Publication
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==Structure of MbQ==
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<StructureSection load='5oja' size='340' side='right' caption='[[5oja]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5oja]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OJA FirstGlance]. <br>
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</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=IMD:IMIDAZOLE'>IMD</scene></td></tr>
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<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=5oja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oja OCA], [http://pdbe.org/5oja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oja RCSB], [http://www.ebi.ac.uk/pdbsum/5oja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oja ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Expanding the range of genetically encoded metal coordination environments accessible within tunable protein scaffolds presents excellent opportunities for the creation of metalloenzymes with augmented properties and novel activities. Here, we demonstrate that installation of a noncanonical Ndelta-methyl histidine (NMH) as the proximal heme ligand in the oxygen binding protein myoglobin (Mb) leads to substantial increases in heme redox potential and promiscuous peroxidase activity. Structural characterization of this catalytically modified myoglobin variant (Mb NMH) revealed significant changes in the proximal pocket, including alterations to hydrogen-bonding interactions involving the prosthetic porphyrin cofactor. Further optimization of Mb NMH via a combination of rational modification and several rounds of laboratory evolution afforded efficient peroxidase biocatalysts within a globin fold, with activities comparable to those displayed by nature's peroxidases.
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Authors: Hayashi, T., Pott, M., Mori, T., Mittl, P., Green, A., Hivert, D.
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A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold.,Pott M, Hayashi T, Mori T, Mittl PRE, Green AP, Hilvert D J Am Chem Soc. 2018 Jan 19. doi: 10.1021/jacs.7b12621. PMID:29309143<ref>PMID:29309143</ref>
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Description: Structure of MbQ
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Hayashi, T]]
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<div class="pdbe-citations 5oja" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Green, A]]
[[Category: Green, A]]
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[[Category: Pott, M]]
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[[Category: Hayashi, T]]
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[[Category: Mori, T]]
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[[Category: Hivert, D]]
[[Category: Hivert, D]]
[[Category: Mittl, P]]
[[Category: Mittl, P]]
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[[Category: Mori, T]]
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[[Category: Pott, M]]
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[[Category: Heme]]
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[[Category: Myoglobin]]
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[[Category: N-methylhistidine]]
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[[Category: Nmh]]
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[[Category: Oxidoreductase]]

Revision as of 18:23, 24 January 2018

Structure of MbQ

5oja, resolution 1.35Å

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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