View source for 4ozk


==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]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ozk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_laterosporus_GI-9 Brevibacillus laterosporus GI-9]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4OZK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.038&#8491;</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=4ozk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozk OCA], [https://pdbe.org/4ozk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ozk RCSB], [https://www.ebi.ac.uk/pdbsum/4ozk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ozk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H1ZZ98_9BACL H1ZZ98_9BACL] 
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ozk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Brevibacillus laterosporus GI-9]]
[[Category: Large Structures]]
[[Category: Thakur KG]]
[[Category: Vipul S]]