1e68: Difference between revisions
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==SOLUTION STRUCTURE OF BACTERIOCIN AS-48== | |||
=== | <StructureSection load='1e68' size='340' side='right' caption='[[1e68]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1e68]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E68 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e68 RCSB], [http://www.ebi.ac.uk/pdbsum/1e68 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Bruix, M | [[Category: Bruix, M]] | ||
[[Category: Galvez, A | [[Category: Galvez, A]] | ||
[[Category: Gonzalez, C | [[Category: Gonzalez, C]] | ||
[[Category: Langdon, G | [[Category: Langdon, G]] | ||
[[Category: Maqueda, M | [[Category: Maqueda, M]] | ||
[[Category: Rico, M | [[Category: Rico, M]] | ||
[[Category: Valdivia, E | [[Category: Valdivia, E]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
[[Category: Bacteriocin]] | [[Category: Bacteriocin]] | ||
Revision as of 20:48, 22 December 2014
SOLUTION STRUCTURE OF BACTERIOCIN AS-48
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