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1e68

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[[Image:1e68.gif|left|200px]]<br /><applet load="1e68" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e68.gif|left|200px]]
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caption="1e68" />
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'''SOLUTION STRUCTURE OF BACTERIOCIN AS-48'''<br />
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{{Structure
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|PDB= 1e68 |SIZE=350|CAPTION= <scene name='initialview01'>1e68</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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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==
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1E68 is a [http://en.wikipedia.org/wiki/Single_protein 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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11005847 11005847]
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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.]]
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[[Category: bacteriocins]]
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[[Category: bacteriocin]]
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[[Category: cationic antibacterial peptides]]
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[[Category: cationic antibacterial peptide]]
[[Category: cyclic polypeptide]]
[[Category: cyclic polypeptide]]
[[Category: five-helixglobule]]
[[Category: five-helixglobule]]
[[Category: nmr solution structure]]
[[Category: nmr solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:16 2008''
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''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


PDB ID 1e68

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Coordinates: save as pdb, mmCIF, xml



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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