6o8r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:56, 14 June 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6o8r is ON HOLD until sometime in the future
+
==Syn-safencin 24==
 +
<StructureSection load='6o8r' size='340' side='right'caption='[[6o8r]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6o8r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_safensis Bacillus safensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O8R FirstGlance]. <br>
 +
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8r OCA], [https://pdbe.org/6o8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o8r RCSB], [https://www.ebi.ac.uk/pdbsum/6o8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8r ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The ribosomally produced antimicrobial peptides of bacteria (bacteriocins) represent an unexplored source of membrane-active antibiotics. We designed a library of linear peptides from a circular bacteriocin and show that pore-formation dynamics in bacterial membranes are tunable via selective amino acid substitution. We observed antibacterial interpeptide synergy indicating that fundamentally altering interactions with the membrane enables synergy. Our findings suggest an approach for engineering pore-formation through rational peptide design and increasing the utility of novel antimicrobial peptides by exploiting synergy.
-
Authors: Fields, F.R., Lee, S.W.
+
Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy.,Fields FR, Manzo G, Hind CK, Janardhanan J, Foik IP, Carmo Silva PD, Balsara RD, Clifford M, Vu HM, Ross JN, Kalwajtys VR, Gonzalez AJ, Bui TT, Ploplis VA, Castellino FJ, Siryaporn A, Chang M, Sutton JM, Mason AJ, Lee S ACS Pharmacol Transl Sci. 2020 Feb 21;3(3):418-424. doi:, 10.1021/acsptsci.0c00001. eCollection 2020 Jun 12. PMID:32566907<ref>PMID:32566907</ref>
-
Description: Syn-safencin 24
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Lee, S.W]]
+
<div class="pdbe-citations 6o8r" style="background-color:#fffaf0;"></div>
-
[[Category: Fields, F.R]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bacillus safensis]]
 +
[[Category: Large Structures]]
 +
[[Category: Fields FR]]
 +
[[Category: Lee SW]]

Current revision

Syn-safencin 24

PDB ID 6o8r

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools