5ojc: Difference between revisions
New page: '''Unreleased structure''' The entry 5ojc is ON HOLD until Paper Publication Authors: Hayashi, T., Pott, M., Mori, T., Mittl, P., Green, A., Hivert, D. Description: Structure of MbQ2.1... |
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==Structure of MbQ2.1 NMH== | |||
<StructureSection load='5ojc' size='340' side='right'caption='[[5ojc]], [[Resolution|resolution]] 1.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ojc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OJC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</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=5ojc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ojc OCA], [https://pdbe.org/5ojc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ojc RCSB], [https://www.ebi.ac.uk/pdbsum/5ojc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ojc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ojc" style="background-color:#fffaf0;"></div> | ||
[[Category: Green | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Physeter catodon]] | |||
[[Category: Green A]] | |||
[[Category: Hayashi T]] | |||
[[Category: Hivert D]] | |||
[[Category: Mittl P]] | |||
[[Category: Mori T]] | |||
[[Category: Pott M]] | |||
Latest revision as of 19:51, 13 December 2023
Structure of MbQ2.1 NMHStructure of MbQ2.1 NMH
Structural highlights
FunctionMYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedExpanding 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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