1e68: Difference between revisions
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1e68 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e68 RCSB]</span> | |||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
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SOLUTION STRUCTURE OF BACTERIOCIN AS-48
Overview
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.
About this Structure
1E68 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
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
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