1e68: Difference between revisions

Line 1:

[[Image:1e68.gif|left|200px]]<br /><applet load="1e68" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1e68.gif|left|200px]]<br /><applet load="1e68" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1e68" />

'''SOLUTION STRUCTURE OF BACTERIOCIN AS-48'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA].

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].

==Reference==

Line 26:

[[Category: nmr solution structure]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sat Nov 24~~ 21:48:~~55 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:16 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1e68.gif|left|200px]]<br /><applet load="1e68" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1e68.gif|left|200px]]<br /><applet load="1e68" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1e68" />
 '''SOLUTION STRUCTURE OF BACTERIOCIN AS-48'''<br />
 ==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.
+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==
-E68 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA].
+E68 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].
 ==Reference==
@@ Line 26: / Line 26: @@
 [[Category: nmr solution structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:48:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:16 2008''