View source for 6aza


==NMR structure of sea anemone toxin Kappa-actitoxin-Ate1a==
<StructureSection load='6aza' size='340' side='right'caption='[[6aza]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6aza]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinia_tenebrosa Actinia tenebrosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AZA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6aza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aza OCA], [https://pdbe.org/6aza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aza RCSB], [https://www.ebi.ac.uk/pdbsum/6aza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aza ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KPHAB_ACTTE KPHAB_ACTTE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sea anemone venoms have long been recognized as a rich source of peptides with interesting pharmacological and structural properties, but they still contain many uncharacterized bioactive compounds. Here we report the discovery, three-dimensional structure, activity, tissue localization, and putative function of a novel sea anemone peptide toxin that constitutes a new, sixth type of voltage-gated potassium channel (KV) toxin from sea anemones. Comprised of just 17 residues, kappa-actitoxin-Ate1a (Ate1a) is the shortest sea anemone toxin reported to date, and it adopts a novel three-dimensional structure that we have named the Proline-Hinged Asymmetric beta-hairpin (PHAB) fold. Mass spectrometry imaging and bioassays suggest that Ate1a serves a primarily predatory function by immobilising prey, and we show this is achieved through inhibition of Shaker-type KV channels. Ate1a is encoded as a multi-domain precursor protein that yields multiple identical mature peptides, which likely evolved by multiple domain duplication events in an actinioidean ancestor. Despite this ancient evolutionary history, the PHAB-encoding gene family exhibits remarkable sequence conservation in the mature peptide domains. We demonstrate that this conservation is likely due to intra-gene concerted evolution, which has to our knowledge not previously been reported for toxin genes. We propose that the concerted evolution of toxin domains provides a hitherto unrecognised way to circumvent the effects of the costly evolutionary arms race considered to drive toxin gene evolution by ensuring efficient secretion of ecologically important predatory toxins.

PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold.,Madio B, Peigneur S, Chin YKY, Hamilton BR, Henriques ST, Smith JJ, Cristofori-Armstrong B, Dekan Z, Boughton BA, Alewood PF, Tytgat J, King GF, Undheim EAB Cell Mol Life Sci. 2018 Aug 14. pii: 10.1007/s00018-018-2897-6. doi:, 10.1007/s00018-018-2897-6. PMID:30109357<ref>PMID:30109357</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aza" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinia tenebrosa]]
[[Category: Large Structures]]
[[Category: Chin YK-Y]]
[[Category: King GF]]
[[Category: Madio B]]
[[Category: Undheim EAB]]