6y2m: Difference between revisions
New page: '''Unreleased structure''' The entry 6y2m is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Streptavidin mutant S112R with a biotC4-1 cofactor - an artificial iron hydroxylase== | ||
<StructureSection load='6y2m' size='340' side='right'caption='[[6y2m]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6y2m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y2M 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]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=O6T:biotC4-1+cofactor'>O6T</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=6y2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2m OCA], [https://pdbe.org/6y2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y2m RCSB], [https://www.ebi.ac.uk/pdbsum/6y2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The selective hydroxylation of C-H bonds is of great interest to the synthetic community. Both homogeneous catalysts and enzymes offer complementary means to tackle this challenge. Herein, we show that biotinylated Fe(TAML)-complexes (TAML = Tetra Amido Macrocyclic Ligand) can be used as cofactors for incorporation into streptavidin to assemble artificial hydroxylases. Chemo-genetic optimization of both cofactor and streptavidin allowed optimizing the performance of the hydroxylase. Using H2O2 as oxidant, up to approximately 300 turnovers for the oxidation of benzylic C-H bonds were obtained. Upgrading the ee was achieved by kinetic resolution of the resulting benzylic alcohol to afford up to >98% ee for (R)-tetralol. X-ray analysis of artificial hydroxylases highlights critical details of the second coordination sphere around the Fe(TAML) cofactor. | |||
Enantioselective Hydroxylation of Benzylic C(sp(3))-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology.,Serrano-Plana J, Rumo C, Rebelein JG, Peterson RL, Barnet M, Ward TR J Am Chem Soc. 2020 Jun 17;142(24):10617-10623. doi: 10.1021/jacs.0c02788. Epub, 2020 Jun 3. PMID:32450689<ref>PMID:32450689</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6y2m" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Avidin 3D structures|Avidin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces avidinii]] | |||
[[Category: Barnet M]] | |||
[[Category: Peterson RL]] | |||
[[Category: Rebelein JG]] | |||
[[Category: Rumo C]] | |||
[[Category: Serrano-Plana J]] | |||
[[Category: Ward TR]] | |||
Latest revision as of 16:18, 24 January 2024
Streptavidin mutant S112R with a biotC4-1 cofactor - an artificial iron hydroxylaseStreptavidin mutant S112R with a biotC4-1 cofactor - an artificial iron hydroxylase
Structural highlights
FunctionSAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedThe selective hydroxylation of C-H bonds is of great interest to the synthetic community. Both homogeneous catalysts and enzymes offer complementary means to tackle this challenge. Herein, we show that biotinylated Fe(TAML)-complexes (TAML = Tetra Amido Macrocyclic Ligand) can be used as cofactors for incorporation into streptavidin to assemble artificial hydroxylases. Chemo-genetic optimization of both cofactor and streptavidin allowed optimizing the performance of the hydroxylase. Using H2O2 as oxidant, up to approximately 300 turnovers for the oxidation of benzylic C-H bonds were obtained. Upgrading the ee was achieved by kinetic resolution of the resulting benzylic alcohol to afford up to >98% ee for (R)-tetralol. X-ray analysis of artificial hydroxylases highlights critical details of the second coordination sphere around the Fe(TAML) cofactor. Enantioselective Hydroxylation of Benzylic C(sp(3))-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology.,Serrano-Plana J, Rumo C, Rebelein JG, Peterson RL, Barnet M, Ward TR J Am Chem Soc. 2020 Jun 17;142(24):10617-10623. doi: 10.1021/jacs.0c02788. Epub, 2020 Jun 3. PMID:32450689[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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