View source for 9foa


==Artificial photoenzyme with anthraquinone cofactor and wild type streptavidin==
<StructureSection load='9foa' size='340' side='right'caption='[[9foa]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9foa]] 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=9FOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FOA 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]] 1.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1ID2:~{N}-[4-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]butyl]-9,10-bis(oxidanylidene)anthracene-2-carboxamide'>A1ID2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=9foa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9foa OCA], [https://pdbe.org/9foa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9foa RCSB], [https://www.ebi.ac.uk/pdbsum/9foa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9foa 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).
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== Publication Abstract from PubMed ==
Artificial metalloenzymes (ArMs) enable the integration of abiotic cofactors within a native protein scaffold, allowing for non-natural catalytic activities. Previous ArMs, however, have primarily relied on single cofactor systems, limiting them to only one catalytic function. Here we present an approach to construct ArMs embedding two catalytic cofactors based on the biotin-streptavidin technology. By incorporating multiple catalytic cofactors into the four binding sites of streptavidin, we engineered programmable ArMs for tandem abiotic transformations including an enantioselective formal C-H hydroxylation and a photooxidation-Michael addition. This work thus outlines a promising strategy for the development of ArMs embedding multiple cofactors.

Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations.,Wang W, Tachibana R, Zhang K, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2025 Jan 6:e202422783. doi: 10.1002/anie.202422783. PMID:39760306<ref>PMID:39760306</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9foa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces avidinii]]
[[Category: Larabi A]]
[[Category: Lau K]]
[[Category: Pojer F]]
[[Category: Wang W]]