6z4r
From Proteopedia
(Difference between revisions)
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==sperm whale myoglobin mutant (H64V V64A) bearing the non-canonical amino acid 3-thienylalanine as axial heme ligand== | ==sperm whale myoglobin mutant (H64V V64A) bearing the non-canonical amino acid 3-thienylalanine as axial heme ligand== | ||
| - | <StructureSection load='6z4r' size='340' side='right'caption='[[6z4r]]' scene=''> | + | <StructureSection load='6z4r' size='340' side='right'caption='[[6z4r]], [[Resolution|resolution]] 1.96Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z4R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6z4r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phymc Phymc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z4R FirstGlance]. <br> |
| - | </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=6z4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z4r OCA], [https://pdbe.org/6z4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z4r RCSB], [https://www.ebi.ac.uk/pdbsum/6z4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z4r ProSAT]</span></td></tr> | + | </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></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Q78:'>Q78</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYMC])</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=6z4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z4r OCA], [https://pdbe.org/6z4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z4r RCSB], [https://www.ebi.ac.uk/pdbsum/6z4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z4r ProSAT]</span></td></tr> | ||
</table> | </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 == | ||
| + | Changing the primary metal coordination sphere is a powerful strategy for tuning metalloprotein properties. Here we used amber stop codon suppression with engineered pyrrolysyl-tRNA synthetases, including two newly evolved enzymes, to replace the proximal histidine in myoglobin with N delta -methylhistidine, 5-thiazoyl-alanine, 4-thiazoylalanine and 3-(3-thienyl)alanine. In addition to tuning the heme redox potential over a >200 mV range, these noncanonical ligands modulate the protein's carbene transfer activity with ethyl diazoacetate. Variants with increased reduction potential proved superior for cyclopropanation and N-H insertion, whereas variants with reduced E o values gave higher S-H insertion activity. Given the functional importance of histidine in many enzymes, these genetically encoded analogues could be valuable tools for probing mechanism and enabling new chemistries. | ||
| + | |||
| + | Noncanonical heme ligands steer carbene transfer reactivity in an artificial metalloenzyme.,Pott M, Tinzl M, Hayashi T, Ota Y, Dunkelmann D, Mittl PRE, Hilvert D Angew Chem Int Ed Engl. 2021 Apr 20. doi: 10.1002/anie.202103437. PMID:33880851<ref>PMID:33880851</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6z4r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hilvert D]] | + | [[Category: Phymc]] |
| - | [[Category: Mittl | + | [[Category: Hilvert, D]] |
| - | [[Category: Tinzl M]] | + | [[Category: Mittl, P R.E]] |
| + | [[Category: Tinzl, M]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Globin]] | ||
| + | [[Category: Heme protein]] | ||
| + | [[Category: Metal binding protein]] | ||
Revision as of 03:46, 2 July 2021
sperm whale myoglobin mutant (H64V V64A) bearing the non-canonical amino acid 3-thienylalanine as axial heme ligand
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