2n86: Difference between revisions
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==NMR structure of OtTx1a - ICK== | ==NMR structure of OtTx1a - ICK== | ||
<StructureSection load='2n86' size='340' side='right' caption='[[2n86 | <StructureSection load='2n86' size='340' side='right'caption='[[2n86]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2n86]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N86 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2n86]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oxyopes_takobius Oxyopes takobius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N86 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n86 OCA], [https://pdbe.org/2n86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n86 RCSB], [https://www.ebi.ac.uk/pdbsum/2n86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SPN1A_OXYTA SPN1A_OXYTA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have recently demonstrated that a common phenomenon in evolution of spider venom composition is the emergence of so-called modular toxins consisting of two domains, each corresponding to a "usual" single-domain toxin. In this article, we describe the structure of two domains that build up a modular toxin named spiderine or OtTx1a from the venom of Oxyopes takobius. Both domains were investigated by solution NMR in water and detergent micelles used to mimic membrane environment. The N-terminal spiderine domain OtTx1a-AMP (41 amino acid residues) contains no cysteines. It is disordered in aqueous solution but in micelles, it assumes a stable amphiphilic structure consisting of two alpha-helices separated by a flexible linker. On the contrary, the C-terminal domain OtTx1a-ICK (59 residues) is a disulfide-rich polypeptide reticulated by five S-S bridges. It presents a stable structure in water and its core is the inhibitor cystine knot (ICK) or knottin motif that is common among single-domain neurotoxins. OtTx1a-ICK structure is the first knottin with five disulfide bridges and it represents a good reference for the whole oxytoxin family. The affinity of both domains to membranes was measured with NMR using titration by liposome suspensions. In agreement with biological tests, OtTx1a-AMP was found to show high membrane affinity explaining its potent antimicrobial properties. | |||
Modular toxin from the lynx spider Oxyopes takobius: Structure of spiderine domains in solution and membrane-mimicking environment.,Nadezhdin KD, Romanovskaia DD, Sachkova MY, Oparin PB, Kovalchuk SI, Grishin EV, Arseniev AS, Vassilevski AA Protein Sci. 2017 Mar;26(3):611-616. doi: 10.1002/pro.3101. Epub 2017 Feb 12. PMID:27997708<ref>PMID:27997708</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2n86" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arseniev | [[Category: Large Structures]] | ||
[[Category: Grishin | [[Category: Oxyopes takobius]] | ||
[[Category: Kovalchuk | [[Category: Arseniev A]] | ||
[[Category: Nadezhdin | [[Category: Grishin E]] | ||
[[Category: Romanovskaya | [[Category: Kovalchuk S]] | ||
[[Category: Sachkova | [[Category: Nadezhdin K]] | ||
[[Category: Vassilevski | [[Category: Romanovskaya D]] | ||
[[Category: Sachkova M]] | |||
[[Category: Vassilevski A]] | |||
Latest revision as of 04:13, 21 November 2024
NMR structure of OtTx1a - ICKNMR structure of OtTx1a - ICK
Structural highlights
FunctionPublication Abstract from PubMedWe have recently demonstrated that a common phenomenon in evolution of spider venom composition is the emergence of so-called modular toxins consisting of two domains, each corresponding to a "usual" single-domain toxin. In this article, we describe the structure of two domains that build up a modular toxin named spiderine or OtTx1a from the venom of Oxyopes takobius. Both domains were investigated by solution NMR in water and detergent micelles used to mimic membrane environment. The N-terminal spiderine domain OtTx1a-AMP (41 amino acid residues) contains no cysteines. It is disordered in aqueous solution but in micelles, it assumes a stable amphiphilic structure consisting of two alpha-helices separated by a flexible linker. On the contrary, the C-terminal domain OtTx1a-ICK (59 residues) is a disulfide-rich polypeptide reticulated by five S-S bridges. It presents a stable structure in water and its core is the inhibitor cystine knot (ICK) or knottin motif that is common among single-domain neurotoxins. OtTx1a-ICK structure is the first knottin with five disulfide bridges and it represents a good reference for the whole oxytoxin family. The affinity of both domains to membranes was measured with NMR using titration by liposome suspensions. In agreement with biological tests, OtTx1a-AMP was found to show high membrane affinity explaining its potent antimicrobial properties. Modular toxin from the lynx spider Oxyopes takobius: Structure of spiderine domains in solution and membrane-mimicking environment.,Nadezhdin KD, Romanovskaia DD, Sachkova MY, Oparin PB, Kovalchuk SI, Grishin EV, Arseniev AS, Vassilevski AA Protein Sci. 2017 Mar;26(3):611-616. doi: 10.1002/pro.3101. Epub 2017 Feb 12. PMID:27997708[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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