1e68: Difference between revisions
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New page: left|200px<br /><applet load="1e68" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e68" /> '''SOLUTION STRUCTURE OF BACTERIOCIN AS-48'''<b... |
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== | ==Solution structure of bacteriocin AS-48== | ||
The solution structure of bacteriocin AS-48, a 70-residue cyclic | <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®/PubMed®, 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: Enterococcus faecalis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bruix | [[Category: Bruix M]] | ||
[[Category: Galvez | [[Category: Galvez A]] | ||
[[Category: Gonzalez | [[Category: Gonzalez C]] | ||
[[Category: Langdon | [[Category: Langdon G]] | ||
[[Category: Maqueda | [[Category: Maqueda M]] | ||
[[Category: Rico | [[Category: Rico M]] | ||
[[Category: Valdivia | [[Category: Valdivia E]] | ||
