1e68
From Proteopedia
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| - | [[Image:1e68.gif|left|200px]] | + | [[Image:1e68.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF BACTERIOCIN AS-48''' | + | {{Structure |
| + | |PDB= 1e68 |SIZE=350|CAPTION= <scene name='initialview01'>1e68</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF BACTERIOCIN AS-48''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E68 is a [ | + | 1E68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11005847 11005847] |
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Rico, M.]] | [[Category: Rico, M.]] | ||
[[Category: Valdivia, E.]] | [[Category: Valdivia, E.]] | ||
| - | [[Category: | + | [[Category: bacteriocin]] |
| - | [[Category: cationic antibacterial | + | [[Category: cationic antibacterial peptide]] |
[[Category: cyclic polypeptide]] | [[Category: cyclic polypeptide]] | ||
[[Category: five-helixglobule]] | [[Category: five-helixglobule]] | ||
[[Category: nmr solution structure]] | [[Category: nmr solution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:24 2008'' |
Revision as of 08:50, 20 March 2008
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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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