9t0x: Difference between revisions

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'''Unreleased structure'''


The entry 9t0x is ON HOLD  until Paper Publication
==Crystal structure of H416C NikA mutant from Escherichia coli covalently bound to a modified Mn(salen) complex==
<StructureSection load='9t0x' size='340' side='right'caption='[[9t0x]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9t0x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9T0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9T0X 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]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LCY:1-METHYLPYRROLIDINE-2,5-DIONE'>LCY</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=9t0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9t0x OCA], [https://pdbe.org/9t0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9t0x RCSB], [https://www.ebi.ac.uk/pdbsum/9t0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9t0x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NIKA_ECOLI NIKA_ECOLI] Involved in a nickel transport system, probably represents the nickel binder.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Artificial enzymes represent a promising alternative for performing non-natural reactions in biocatalysis. Here, we illustrate the potential of cross-linked enzyme crystals (CLEC) to achieve enantioselective epoxidation through the generation of an artificial enzyme obtained by direct covalent anchoring of a manganese complex as an artificial active site within a protein. Enantiomeric excess (ee) of up to 90% on cis-beta-methylstyrene was measured when the covalent binding yield was maximized, thanks to the remarkable behavior of the crystals. The structure of the modified enzyme, NikA, is provided. This work adds to the growing body of examples highlighting the advantages of CLEC in oxidation catalysis.


Authors:  
Covalent Insertion of a Mn(Salen) Type Complex in Cross-Linked Protein Crystals: Design of an Enantioselective Artificial Epoxidase.,Boukhallat M, Benhamed I, Arnone J, Van Baaren S, Rinaldi C, Catty P, Marchi-Delapierre C, Cavazza C, Menage S Chemistry. 2026 May 29:e71159. doi: 10.1002/chem.71159. PMID:42210913<ref>PMID:42210913</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9t0x" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Cavazza C]]
[[Category: Menage S]]