View source for 5mml


==HYL-20k==
<StructureSection load='5mml' size='340' side='right'caption='[[5mml]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hylaeus_signatus Hylaeus signatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MML FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5mml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mml OCA], [https://pdbe.org/5mml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mml RCSB], [https://www.ebi.ac.uk/pdbsum/5mml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mml ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
HYL-20 (GILSSLWKKLKKIIAK-NH2) is an analogue of a natural antimicrobial peptide (AMP) previously isolated from the venom of wild bee. We examined its antimicrobial activity against three strains of Enterococcus faecalis while focusing on its susceptibility to proteolytic degradation by two known proteases-gelatinase (GelE) and serine protease (SprE)-which are secreted by these bacterial strains. We found that HYL-20 was primarily deamidated at its C-terminal which made the peptide susceptible to consecutive intramolecular cleavage by GelE. Further study utilising 1,10-phenanthroline, a specific GelE inhibitor and analogous peptide with D-Lys at its C-terminus (HYL-20k) revealed that the C-terminal deamidation of HYL-20 is attributed to not yet unidentified protease which also cleaves internal peptide bonds of AMPs. In contrast to published data, participation of SprE in the protective mechanism of E. faecalis against AMPs was not proved. The resistance of HYL-20k to C-terminal deamidation and subsequent intramolecular cleavage has resulted in increased antimicrobial activity against E. faecalis grown in planktonic and biofilm form when compared to HYL-20.

How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides.,Nesuta O, Budesinsky M, Hadravova R, Monincova L, Humpolickova J, Cerovsky V Pathog Dis. 2017 Sep 29;75(7). doi: 10.1093/femspd/ftx091. PMID:28830077<ref>PMID:28830077</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mml" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Hylaeus signatus]]
[[Category: Large Structures]]
[[Category: Hexnerova R]]