5cog: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5cog" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Crystal structure of Yeast IRC4== | ||
<StructureSection load='5cog' size='340' side='right' caption='[[5cog]], [[Resolution|resolution]] 1.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cog]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5COG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cog OCA], [http://pdbe.org/5cog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cog RCSB], [http://www.ebi.ac.uk/pdbsum/5cog 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5cog" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Matthews, S J]] | |||
[[Category: Taylor, J D]] | |||
[[Category: Cell cycle]] | |||
[[Category: Duf1706]] | |||
[[Category: Unknown function]] | |||