1AMT
Crystal structure of alamethicin at 1.5 angstrom resolution
Summary for 1AMT
| Entry DOI | 10.2210/pdb1amt/pdb |
| Related | 1DLZ 1EE7 1GQ0 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U |
| Related PRD ID | PRD_000163 |
| Descriptor | ALAMETHICIN F30, ACETONITRILE, METHANOL (3 entities in total) |
| Functional Keywords | alamethicin, peptaibol, antibacterial, antifungal, antibiotic |
| Biological source | TRICHODERMA VIRIDE |
| Total number of polymer chains | 3 |
| Total formula weight | 6343.58 |
| Authors | Fox, R.O.,Richards, F.M. (deposition date: 1987-12-08, release date: 1988-10-09, Last modification date: 2025-03-26) |
| Primary citation | Fox Jr, R.O.,Richards, F.M. A Voltage-Gated Ion Channel Model Inferred from the Crystal Structure of Alamethicin at 1.5-A Resolution. Nature, 300:325-, 1982 Cited by PubMed Abstract: The crystal structure of alamethicin in nonaqueous solvent has been determined, and refined at 1.5-A resolution. The molecular conformation of the three crystallographically independent molecules is largely alpha-helical with a bend in the helix axis at an internal proline residue. The helix structure is highly amphipathic as most of the solvent-accessible polar atoms lie on a narrow strip of surface parallel to the helix axis. Molecular models for the voltage-gated ion channel, with n-fold symmetry and based on the molecular conformations observed in the crystal, are characterized by strong surface complementarity, a hydrophilic interior and a hydrophobic exterior. The channel structures are stabilized by a hydrated annulus of hydrogen-bonded glutamine residues which produce the greatest restriction in the channel diameter. PubMed: 6292726DOI: 10.1038/300325A0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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