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==Structure of 6-aminohexanoate-oligomer hydrolase NylC precursor, D122G/H130Y/T267C mutant==
<StructureSection load='7yu1' size='340' side='right'caption='[[7yu1]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yu1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter Arthrobacter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YU1 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]] 1.13&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7yu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yu1 OCA], [https://pdbe.org/7yu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yu1 RCSB], [https://www.ebi.ac.uk/pdbsum/7yu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yu1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NYLC_FLASK NYLC_FLASK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nylon hydrolase (NylC), a member of the N-terminal nucleophile (Ntn) hydrolase superfamily, is responsible for the degradation of various aliphatic nylons, including nylon-6 and nylon-66. NylC is initially expressed as an inactive precursor (36 kDa), but the precursor is autocatalytically cleaved at Asn266/Thr267 to generate an active enzyme composed of 27 and 9 kDa subunits. We isolated various mutants with amino acid changes at the catalytic centre. X-ray crystallographic analysis revealed that the NylC precursor forms a doughnut-shaped quaternary structure composed of four monomers (molecules A-D) with D2 symmetry. Catalytic residues in the precursor are covered by loop regions at the A/B interface (equivalent to the C/D interface). However, the catalytic residues are exposed to the solvent environment through autocleavage followed by movements of the loop regions. T267A, D306A and D308A mutations resulted in a complete loss of autocleavage. By contrast, in the T267S mutant, autocleavage proceeded slowly at a constant reaction rate (k = 2.8 x 10(-5) s(-1) ) until complete conversion, but the reaction was inhibited by K189A and N219A mutations. Based on the crystallographic and molecular dynamic simulation analyses, we concluded that the Asp308-Asp306-Thr267 triad, resembling the Glu-Ser-Ser triad conserved in Ntn-hydrolase family enzymes, is responsible for autocleavage and that hydrogen-bonding networks connecting Thr267 with Lys189 and Asn219 are required for increasing the nucleophilicity of Thr267-OH in both the water accessible and water inaccessible systems. Furthermore, we determined that NylC employs the Asp308-Asp306-Thr267 triad as catalytic residues for substrate hydrolysis, but the reaction requires Lys189 and Tyr146 as additional catalytic/substrate-binding residues specific for nylon hydrolysis.

X-ray crystallographic and mutational analysis of the NylC precursor: catalytic mechanism of autocleavage and substrate hydrolysis of nylon hydrolase.,Negoro S, Shibata N, Kato DI, Tanaka Y, Yasuhira K, Nagai K, Oshima S, Furuno Y, Yokoyama R, Miyazaki K, Takeo M, Hengphasatporn K, Shigeta Y, Lee YH, Higuchi Y FEBS J. 2023 Feb 17. doi: 10.1111/febs.16755. PMID:36799721<ref>PMID:36799721</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yu1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Arthrobacter]]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Negoro S]]