5oj9: Difference between revisions
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==Structure of Mb NMH== | ==Structure of Mb NMH== | ||
<StructureSection load='5oj9' size='340' side='right' caption='[[5oj9]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='5oj9' size='340' side='right'caption='[[5oj9]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oj9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJ9 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5oj9]] 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=5OJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OJ9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.483Å</td></tr> | ||
<tr id=' | <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=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oj9 OCA], [https://pdbe.org/5oj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oj9 RCSB], [https://www.ebi.ac.uk/pdbsum/5oj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oj9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5oj9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5oj9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Physeter catodon]] | ||
[[Category: | [[Category: Green A]] | ||
[[Category: | [[Category: Hayashi T]] | ||
[[Category: Hivert D]] | |||
[[Category: | [[Category: Mittl P]] | ||
[[Category: | [[Category: Mori T]] | ||
[[Category: | [[Category: Pott M]] | ||
[[Category: | |||
Latest revision as of 19:51, 13 December 2023
Structure of Mb NMHStructure of Mb 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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