View source for 1e68


==Solution structure of bacteriocin AS-48==
<StructureSection load='1e68' size='340' side='right'caption='[[1e68]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E68 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e68 OCA], [https://pdbe.org/1e68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e68 RCSB], [https://www.ebi.ac.uk/pdbsum/1e68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e68 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47765_ENTFL Q47765_ENTFL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of bacteriocin AS-48, a 70-residue cyclic polypeptide from Enterococcus faecalis, consists of a globular arrangement of five alpha-helices enclosing a compact hydrophobic core. The head-to-tail union lies in the middle of helix 5, a fact that is shown to have a pronounced effect on the stability of the three-dimensional structure. Positive charges in the side chains of residues in helix 4 and in the turn linking helix 4 to helix 5 form a cluster that most probably determine its antibacterial activity by promoting pore formation in cell membranes. A similar five-helix structural motif has been found in the antimicrobial NK-lysin, an effector polypeptide of T and natural killer (NK) cells. Bacteriocin AS-48 lacks the three disulfide bridges characteristic of the saposin fold present in NK-lysin, and has no sequence homology with it. Nevertheless, the similar molecular architecture and high positive charge strongly suggest a common mechanism of antibacterial action.

Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.,Gonzalez C, Langdon GM, Bruix M, Galvez A, Valdivia E, Maqueda M, Rico M Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6. PMID:11005847<ref>PMID:11005847</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1e68" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Bruix M]]
[[Category: Galvez A]]
[[Category: Gonzalez C]]
[[Category: Langdon G]]
[[Category: Maqueda M]]
[[Category: Rico M]]
[[Category: Valdivia E]]