1GQ0
Solution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structures
Summary for 1GQ0
| Entry DOI | 10.2210/pdb1gq0/pdb |
| Related | 1AMT 1DLZ 1EE7 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U |
| Related PRD ID | PRD_000161 |
| Descriptor | ANTIAMOEBIN I (1 entity in total) |
| Functional Keywords | antiamoebin i, peptaibol, antibacterial, antifungal, antibiotic |
| Biological source | EMERICELLOPSIS SP. 2723 |
| Total number of polymer chains | 1 |
| Total formula weight | 1654.99 |
| Authors | Galbraith, T.P.,Harris, R.,Driscoll, P.C.,Wallace, B.A. (deposition date: 2001-11-16, release date: 2003-01-24, Last modification date: 2017-12-20) |
| Primary citation | Galbraith, T.P.,Harris, R.,Driscoll, P.C.,Wallace, B.A. Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide. Biophys. J., 84:185-194, 2003 Cited by PubMed Abstract: Antiamoebin I is a membrane-active peptaibol produced by fungi of the species Emericellopsis which is capable of forming ion channels in membranes. Previous structure determinations by x-ray crystallography have shown the molecule is mostly helical, with a deep bend in the center of the polypeptide, and that the backbone structure is independent of the solvent used for crystallization. In this study, the solution structure of antiamoebin was determined by NMR spectroscopy in methanol, a solvent from which one of the crystal structures was determined. The ensemble of structures produced exhibit a right-handed helical C terminus and a left-handed helical conformation toward the N-terminus, in contrast to the completely right-handed helices found in the crystal structures. The NMR results also suggest that a "hinge" region exists, which gives flexibility to the polypeptide in the central region, and which could have functional implications for the membrane insertion process. A model for the membrane insertion and assembly process is proposed based on the antiamoebin solution and crystal structures, and is contrasted with the assembly and insertion mechanism proposed for other ion channel-forming polypeptides. PubMed: 12524274DOI: 10.1016/S0006-3495(03)74841-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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