1ED0
NMR structural determination of viscotoxin A3 from Viscum album L.
Summary for 1ED0
| Entry DOI | 10.2210/pdb1ed0/pdb |
| Related | 1ab1 1bhp 1cbn 1ccm 1cnr 2plh |
| NMR Information | BMRB: 4587 |
| Descriptor | VISCOTOXIN A3 (1 entity in total) |
| Functional Keywords | thionin, concentric motif, helix-turn-helix, alpha-beta protein, amphipathic helix, toxin |
| Biological source | Viscum album (European mistletoe) |
| Total number of polymer chains | 1 |
| Total formula weight | 4842.63 |
| Authors | Romagnoli, S.,Ugolini, R.,Fogolari, F.,Schaller, G.,Urech, K.,Giannattasio, M.,Ragona, L.,Molinari, H. (deposition date: 2000-01-26, release date: 2000-02-04, Last modification date: 2024-11-06) |
| Primary citation | Romagnoli, S.,Ugolini, R.,Fogolari, F.,Schaller, G.,Urech, K.,Giannattasio, M.,Ragona, L.,Molinari, H. NMR structural determination of viscotoxin A3 from Viscum album L. Biochem.J., 350:569-577, 2000 Cited by PubMed Abstract: The high-resolution three-dimensional structure of the plant toxin viscotoxin A3, from Viscum album L., has been determined in solution by (1)H NMR spectroscopy at pH 3.6 and 12 degrees C (the structure has been deposited in the Protein Data Bank under the id. code 1ED0). Experimentally derived restraints including 734 interproton distances from nuclear Overhauser effect measurements, 22 hydrogen bonds, 32 φ angle restraints from J coupling measurements, together with three disulphide bridge constraints were used as input in restrained molecular dynamics, followed by minimization, using DYANA and Discover. Backbone and heavy atom root-mean-square deviations were 0.47+/-0.11 A (1 A=10(-10) m) and 0.85+/-0.13 A respectively. Viscotoxin A3 consists of two alpha-helices connected by a turn and a short stretch of antiparallel beta-sheet. This fold is similar to that found in other thionins, such as crambin, hordothionin-alpha and -beta, phoratoxin A and purothionin-alpha and -beta. The difference in the observed biological activity for thionins of known structure is discussed in terms of the differences in the calculated surface potential distribution, playing an important role in their function through disruption of cell membranes. In addition, the possible role in DNA binding of the helix-turn-helix motif of viscotoxin A3 is discussed. PubMed: 10947973DOI: 10.1042/0264-6021:3500569 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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