8sm6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Aerobic, Diiron(III)-metalated SfbO== | |
| + | <StructureSection load='8sm6' size='340' side='right'caption='[[8sm6]], [[Resolution|resolution]] 1.39Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8sm6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Litorilinea_aerophila Litorilinea aerophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SM6 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]] 1.39Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8sm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sm6 OCA], [https://pdbe.org/8sm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sm6 RCSB], [https://www.ebi.ac.uk/pdbsum/8sm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sm6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A540VG95_9CHLR A0A540VG95_9CHLR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dinuclear monooxygenases mediate challenging C-H bond oxidation reactions throughout nature. Many of these enzymes are presumed to exclusively utilize diiron cofactors. Herein we report the bioinformatic discovery of an orphan dinuclear monooxygenase that preferentially utilizes a heterobimetallic manganese-iron (Mn/Fe) cofactor to mediate an O(2)-dependent C-H bond hydroxylation reaction. Unlike the structurally similar Mn/Fe-dependent monooxygenase AibH2, the diiron form of this enzyme (SfbO) exhibits a nascent enzymatic activity. This behavior raises the possibility that many other dinuclear monooxygenases may be endowed with the capacity to harness cofactors with a variable metal content. | ||
| - | + | Bioinformatic Discovery of a Cambialistic Monooxygenase.,Liu C, Powell MM, Rao G, Britt RD, Rittle J J Am Chem Soc. 2024 Jan 24;146(3):1783-1788. doi: 10.1021/jacs.3c12131. Epub 2024 , Jan 10. PMID:38198693<ref>PMID:38198693</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8sm6" style="background-color:#fffaf0;"></div> |
| - | [[Category: Liu | + | == References == |
| - | [[Category: Powell | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Litorilinea aerophila]] | ||
| + | [[Category: Liu C]] | ||
| + | [[Category: Powell MM]] | ||
| + | [[Category: Rittle J]] | ||
Current revision
Aerobic, Diiron(III)-metalated SfbO
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