5com: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of Uncharacterized Protein Q187F5 from Clostridium difficile 630==
<StructureSection load='5com' size='340' side='right' caption='[[5com]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5com]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5COM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5COM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5com FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5com OCA], [http://pdbe.org/5com PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5com RCSB], [http://www.ebi.ac.uk/pdbsum/5com PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria have developed a variety of mechanisms for surviving harsh environmental conditions, nutrient stress and overpopulation. Paenibacillus dendritiformis produces a lethal protein (Slf) that is able to induce cell death in neighbouring colonies and a phenotypic switch in more distant ones. Slf is derived from the secreted precursor protein, DfsB, after proteolytic processing. Here, we present new crystal structures of DfsB homologues from a variety of bacterial species and a surprising version present in the yeast Saccharomyces cerevisiae. Adopting a four-helix bundle decorated with a further three short helices within intervening loops, DfsB belongs to a non-enzymatic class of the DinB fold. The structure suggests that the biologically active Slf fragment may possess a C-terminal helix rich in basic and aromatic residues that suggest a functional mechanism akin to that for cationic antimicrobial peptides.


The entry 5com is ON HOLD  until Paper Publication
Structures of the DfsB Protein Family Suggest a Cationic, Helical Sibling Lethal Factor Peptide.,Taylor JD, Taylor G, Hare SA, Matthews SJ J Mol Biol. 2016 Jan 21. pii: S0022-2836(16)00032-2. doi:, 10.1016/j.jmb.2016.01.013. PMID:26804569<ref>PMID:26804569</ref>


Authors: Taylor, J.D., Taylor, G., Matthews, S.J.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description:  
<div class="pdbe-citations 5com" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Matthews, S.J]]
<references/>
__TOC__
</StructureSection>
[[Category: Matthews, S J]]
[[Category: Taylor, G]]
[[Category: Taylor, G]]
[[Category: Taylor, J.D]]
[[Category: Taylor, J D]]
[[Category: Dfsb]]
[[Category: Duf1706]]
[[Category: Replication]]
[[Category: Unknown function]]
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