1e68
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1e68.gif|left|200px]] | [[Image:1e68.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1e68", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_1e68| PDB=1e68 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''SOLUTION STRUCTURE OF BACTERIOCIN AS-48''' | '''SOLUTION STRUCTURE OF BACTERIOCIN AS-48''' | ||
Line 32: | Line 29: | ||
[[Category: Rico, M.]] | [[Category: Rico, M.]] | ||
[[Category: Valdivia, E.]] | [[Category: Valdivia, E.]] | ||
- | [[Category: | + | [[Category: Bacteriocin]] |
- | [[Category: | + | [[Category: Cationic antibacterial peptide]] |
- | [[Category: | + | [[Category: Cyclic polypeptide]] |
- | [[Category: | + | [[Category: Five-helixglobule]] |
- | [[Category: | + | [[Category: Nmr solution structure]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:53 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 11:42, 2 May 2008
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 Page seeded by OCA on Fri May 2 14:42:53 2008