9sx8: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 9sx8 is ~~ON HOLD until Paper~~ Publication

==Crystal structure of eSNAr1.3 (K39A) in complex with 2,4-dinitrobromobenzene==

== Structural highlights ==

<table><tr><td colspan='2'>[[9sx8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SX8 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]] 2.1Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1JRE:1-bromanyl-2,4-dinitro-benzene'>A1JRE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=9sx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9sx8 OCA], [https://pdbe.org/9sx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9sx8 RCSB], [https://www.ebi.ac.uk/pdbsum/9sx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9sx8 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Enzymes that catalyze non-natural C-C bond-forming reactions are powerful tools in asymmetric synthesis, yet reprogramming their active sites to invert stereochemical outcome remains challenging. Building on our recently engineered S(N)Arase, S(N)Ar1.3, which performs enantioselective nucleophilic aromatic substitutions with carbon nucleophiles, we now report the evolution of an enantiocomplementary biocatalyst (eS(N)Ar1.3) that displays enhanced activity and expanded substrate scope. Structural and computational analyses uncover both conserved and divergent features between S(N)Ar1.3 and eS(N)Ar1.3. Despite retaining similar electrophile binding poses and a conserved catalytic arginine, the halide-binding pocket of S(N)Ar1.3 has been abandoned in eS(N)Ar1.3. Instead, His23 has emerged as a key motif that works with Arg124 to accurately position the nucleophilic substrate. Calculations reveal that Arg124 also plays a crucial role in facilitating halide release during catalysis. Our study demonstrates how evolution can reshape enzyme mechanisms in unforeseen ways, highlighting the importance of exploring diverse trajectories to access new functions.

~~Authors:~~ Roberts, G.R.~~, Leys, D~~.

Directed evolution of an enantiocomplementary S(N)Arase reveals divergent catalytic features.,Lister TM, Roberts GW, Duran C, Casadevall G, Zhao F, Millman AAV, Larrosa I, Osuna S, Green AP Nat Commun. 2026 Aug 21;17(1):10033. doi: 10.1038/s41467-026-76922-5. PMID:42767999<ref>PMID:42767999</ref>

~~Description: Crystal structure~~ of ~~eSNAr1~~.~~3 (K39A) in complex with 2,4~~-~~dinitrobromobenzene~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Leys, D]]

[[Category: Roberts~~, G.R~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Leys D]]

[[Category: Roberts GR]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9sx8 is ON HOLD  until Paper Publication
+==Crystal structure of eSNAr1.3 (K39A) in complex with 2,4-dinitrobromobenzene==
+<StructureSection load='9sx8' size='340' side='right'caption='[[9sx8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9sx8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SX8 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1JRE:1-bromanyl-2,4-dinitro-benzene'>A1JRE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=9sx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9sx8 OCA], [https://pdbe.org/9sx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9sx8 RCSB], [https://www.ebi.ac.uk/pdbsum/9sx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9sx8 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enzymes that catalyze non-natural C-C bond-forming reactions are powerful tools in asymmetric synthesis, yet reprogramming their active sites to invert stereochemical outcome remains challenging. Building on our recently engineered S(N)Arase, S(N)Ar1.3, which performs enantioselective nucleophilic aromatic substitutions with carbon nucleophiles, we now report the evolution of an enantiocomplementary biocatalyst (eS(N)Ar1.3) that displays enhanced activity and expanded substrate scope. Structural and computational analyses uncover both conserved and divergent features between S(N)Ar1.3 and eS(N)Ar1.3. Despite retaining similar electrophile binding poses and a conserved catalytic arginine, the halide-binding pocket of S(N)Ar1.3 has been abandoned in eS(N)Ar1.3. Instead, His23 has emerged as a key motif that works with Arg124 to accurately position the nucleophilic substrate. Calculations reveal that Arg124 also plays a crucial role in facilitating halide release during catalysis. Our study demonstrates how evolution can reshape enzyme mechanisms in unforeseen ways, highlighting the importance of exploring diverse trajectories to access new functions.
-Authors: Roberts, G.R., Leys, D.
+Directed evolution of an enantiocomplementary S(N)Arase reveals divergent catalytic features.,Lister TM, Roberts GW, Duran C, Casadevall G, Zhao F, Millman AAV, Larrosa I, Osuna S, Green AP Nat Commun. 2026 Aug 21;17(1):10033. doi: 10.1038/s41467-026-76922-5. PMID:42767999<ref>PMID:42767999</ref>
-Description: Crystal structure of eSNAr1.3 (K39A) in complex with 2,4-dinitrobromobenzene
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Leys, D]]
+<div class="pdbe-citations 9sx8" style="background-color:#fffaf0;"></div>
-[[Category: Roberts, G.R]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Leys D]]
+[[Category: Roberts GR]]