4ozk: Difference between revisions
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''' | ==Crystal structure of Laterosporulin, a broad spectrum leaderless bacteriocin produced by Brevibacillus laterosporus strain GI-9== | ||
<StructureSection load='4ozk' size='340' side='right' caption='[[4ozk]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ozk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_laterosporus Brevibacillus laterosporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OZK FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ozk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ozk RCSB], [http://www.ebi.ac.uk/pdbsum/4ozk PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The growing emergence of antibiotic-resistant bacteria has led to exploring naturally occurring defense peptides as antimicrobials. In this study, we report that laterosporulin, a class IId bacteriocin, effectively kills active and non-multiplying cells of both Gram-positive and Gram-negative bacteria. Fluorescence and electron microscopy suggest that growth inhibition occurs due to increased membrane permeability. Crystal structure of laterosporulin at 2.0 A resolution reveals an all-beta conformation of this peptide with four beta strands forming a twisted beta-sheet. All the six intrinsic cysteine residues are intramolecularly disulfide bonded with two disulfides constraining the N-terminus of the peptide and the third disulfide crosslinks the extreme C-terminus resulting in the formation of a closed structure. Significance of disulfides in maintaining the in-solution peptide structure was confirmed by the circular dichroism and fluorescence analyses. Despite a low overall sequence similarity, laterosporulin has the disulfide connectivity [CI -CV , CII -CIV , CIII -CVI ] like beta-defensins and a striking architectural similarity with alpha-defensins. Therefore laterosporulin presents a missing link between bacteriocins and mammalian defensins and is also a potential antimicrobial lead, in particular against non-multiplying bacteria. This article is protected by copyright. All rights reserved. | |||
Intra-molecular Disulfide-Stapled Structure of Laterosporulin, a Class IId Bacteriocin, Conceals Human Defensin-like Structural Module.,Singh PK, Solanki V, Sharma S, Thakur KG, Krishnan B, Korpole S FEBS J. 2014 Oct 27. doi: 10.1111/febs.13129. PMID:25345978<ref>PMID:25345978</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevibacillus laterosporus]] | |||
[[Category: Thakur, K G]] | |||
[[Category: Vipul, S]] | |||
[[Category: Antimicrobial]] | |||
[[Category: Bacteriocin]] | |||
[[Category: Class iid]] | |||
[[Category: Defensin-like]] | |||
[[Category: Heat stable]] | |||
[[Category: Leaderless]] | |||
[[Category: Toxin]] | |||
