2N85
NMR structure of OtTx1a - AMP in DPC micelles
Summary for 2N85
| Entry DOI | 10.2210/pdb2n85/pdb |
| Related | 2N86 |
| NMR Information | BMRB: 25835 |
| Descriptor | Spiderine-1a (1 entity in total) |
| Functional Keywords | spider venom, n-terminal end, dpc micelles, toxin |
| Biological source | Oxyopes takobius (Lynx spider) |
| Total number of polymer chains | 1 |
| Total formula weight | 4832.00 |
| Authors | Nadezhdin, K.,Romanovskaya, D.,Sachkova, M.,Vassilevski, A.,Grishin, E.,Kovalchuk, S.,Arseniev, A. (deposition date: 2015-10-05, release date: 2016-10-05, Last modification date: 2024-05-15) |
| Primary citation | Nadezhdin, K.D.,Romanovskaia, D.D.,Sachkova, M.Y.,Oparin, P.B.,Kovalchuk, S.I.,Grishin, E.V.,Arseniev, A.S.,Vassilevski, A.A. Modular toxin from the lynx spider Oxyopes takobius: Structure of spiderine domains in solution and membrane-mimicking environment. Protein Sci., 26:611-616, 2017 Cited by PubMed Abstract: 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 α-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. PubMed: 27997708DOI: 10.1002/pro.3101 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
