5T8A
Recombinant cytotoxin-I from the venom of cobra N. oxiana
Summary for 5T8A
| Entry DOI | 10.2210/pdb5t8a/pdb |
| Related | 1RL5 1ZAD |
| NMR Information | BMRB: 30172 |
| Descriptor | Cytotoxin 1 (1 entity in total) |
| Functional Keywords | toxin, cytolytic peptide, all-beta sheet protein, recombinant production, structure from molmol |
| Biological source | Naja oxiana (Central Asian cobra) |
| Total number of polymer chains | 1 |
| Total formula weight | 6962.53 |
| Authors | Dubovskii, P.V.,Dubinnyi, M.A.,Shulepko, M.A.,Lyukmanova, E.N.,Dolgikh, D.A.,Kirpichnikov, M.P.,Efremov, R.G. (deposition date: 2016-09-07, release date: 2017-09-20, Last modification date: 2019-05-08) |
| Primary citation | Dubovskii, P.V.,Dubinnyi, M.A.,Konshina, A.G.,Kazakova, E.D.,Sorokoumova, G.M.,Ilyasova, T.M.,Shulepko, M.A.,Chertkova, R.V.,Lyukmanova, E.N.,Dolgikh, D.A.,Arseniev, A.S.,Efremov, R.G. Structural and Dynamic "Portraits" of Recombinant and Native Cytotoxin I from Naja oxiana: How Close Are They? Biochemistry, 56:4468-4477, 2017 Cited by PubMed Abstract: Today, recombinant proteins are quite widely used in biomedical and biotechnological applications. At the same time, the question about their full equivalence to the native analogues remains unanswered. To gain additional insight into this problem, intimate atomistic details of a relatively simple protein, small and structurally rigid recombinant cardiotoxin I (CTI) from cobra Naja oxiana venom, were characterized using nuclear magnetic resonance (NMR) spectroscopy and atomistic molecular dynamics (MD) simulations in water. Compared to the natural protein, it contains an additional Met residue at the N-terminus. In this work, the NMR-derived spatial structure of uniformly C- and N-labeled CTI and its dynamic behavior were investigated and subjected to comparative analysis with the corresponding data for the native toxin. The differences were found in dihedral angles of only a single residue, adjacent to the N-terminal methionine. Microsecond-long MD traces of the toxins reveal an increased flexibility in the residues spatially close to the N-Met. As the detected structural and dynamic changes of the two CTI models do not result in substantial differences in their cytotoxicities, we assume that the recombinant protein can be used for many purposes as a reasonable surrogate of the native one. In addition, we discuss general features of the spatial organization of cytotoxins, implied by the results of the current combined NMR and MD study. PubMed: 28749688DOI: 10.1021/acs.biochem.7b00453 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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