View source for 4nsy


==Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK==
<StructureSection load='4nsy' size='340' side='right'caption='[[4nsy]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nsy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NSY 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]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OY:N-[(2S,3S)-7-AMINO-1-CHLORO-2-HYDROXYHEPTAN-3-YL]-4-METHYLBENZENESULFONAMIDE+(BOUND+FORM)'>2OY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4nsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nsy OCA], [https://pdbe.org/4nsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nsy RCSB], [https://www.ebi.ac.uk/pdbsum/4nsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nsy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_LYSEN LYSC_LYSEN] Highly specific endopeptidase that hydrolyzes lysyl bonds including the Lys-Pro bond.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lysobacter enzymogenes lysyl endoproteinase (LysC) is a trypsin-type serine protease with a high pH optimum that hydrolyses all Lys-Xaa peptide bonds. The high specificity of LysC renders it useful for biotechnological purposes. The K30R variant of a related lysyl endoproteinase from Achromobacter lyticus has favourable enzymatic properties that might be transferrable to LysC. To visualize structural differences in the substrate-binding sites, the crystal structures of wild-type and the K30R variant of LysC were determined. The mutation is located at a distance of 12 A from the catalytic triad and subtly changes the surface properties of the substrate-binding site. The high pH optimum of LysC can be attributed to electrostatic effects of an aromatic Tyr/His stack on the catalytic aspartate and is a general feature of this enzyme subfamily. LysC crystals in complex with the covalent inhibitor N(alpha)-p-tosyl-lysyl chloromethylketone yielded data to 1.1 and 0.9 A resolution, resulting in unprecedented precision of the active and substrate-binding sites for this enzyme subfamily. Error estimates on bond lengths and difference electron density indicate that instead of the expected oxyanion a hydroxyl group binds to the partially solvent-exposed oxyanion hole. Protonation of the alkoxide catalytic intermediate might be a recurring feature during serine protease catalysis.

Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole.,Asztalos P, Muller A, Holke W, Sobek H, Rudolph MG Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1832-43. doi:, 10.1107/S1399004714008463. Epub 2014 Jun 29. PMID:25004961<ref>PMID:25004961</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nsy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Lysobacter enzymogenes]]
[[Category: Asztalos P]]
[[Category: Holke W]]
[[Category: Muller A]]
[[Category: Rudolph MG]]
[[Category: Sobek H]]