View source for 9cxr


==X-ray Crystallographic Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 at Room Temperature==
<StructureSection load='9cxr' size='340' side='right'caption='[[9cxr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cxr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alphaproteobacteria_bacterium Alphaproteobacteria bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CXR 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=9cxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cxr OCA], [https://pdbe.org/9cxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cxr RCSB], [https://www.ebi.ac.uk/pdbsum/9cxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cxr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A522DD61_9PROT A0A522DD61_9PROT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes have evolved to rapidly and selectively hydrolyze diverse natural and anthropogenic polymers, but only a limited group of related enzymes have been shown to hydrolyze synthetic polyamides. In this work, we synthesized and characterized a panel of 95 diverse enzymes from the N-terminal nucleophile hydrolase superfamily with 30-50% pairwise amino acid identity. We found that nearly 40% of the enzymes had substantial nylon hydrolase activity, in many cases comparable to that of the best-characterized nylon hydrolase, NylC. There was no relationship between phylogeny and activity, nor any evidence of prior selection for nylon hydrolase activity. Several newly-identified hydrolases showed significant substrate selectivity, generating up to 20-fold higher product titers with Nylon 6,6 versus Nylon 6. Finally, we determined the crystal structure and oligomerization state of a Nylon 6,6-selective hydrolase to elucidate structural factors that could affect activity and selectivity. These new enzymes provide insights into the widespread potential for nylon hydrolase evolution and opportunities for analysis and engineering of improved hydrolases.

Identification and characterization of substrate- and product-selective nylon hydrolases.,Drufva EE, Cahill JF, Saint-Vincent PMB, Williams AN, Bocharova V, Capra N, Meilleur F, Carper DL, Bourgery C, Miyazaki K, Yonemura M, Shiraishi Y, Parks JM, Zhou M, Dishner IT, Foster JC, Koehler SJ, Valentino HR, Sedova A, Kertesz V, Vasileva DP, Hochanadel LH, Figg CA, Negoro S, Kato DI, Chen SH, Michener JK bioRxiv [Preprint]. 2024 Nov 14:2024.11.14.623603. doi: , 10.1101/2024.11.14.623603. PMID:39605696<ref>PMID:39605696</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cxr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alphaproteobacteria bacterium]]
[[Category: Large Structures]]
[[Category: Chen SH]]
[[Category: Drufva EE]]
[[Category: Meilleur F]]
[[Category: Michener JK]]
[[Category: Parks JM]]
[[Category: Williams AN]]