Crystal structure of alamethicin at 1.5 angstrom resolutionCrystal structure of alamethicin at 1.5 angstrom resolution

Structural highlights

1amt is a 3 chain structure with sequence from Trichoderma viride. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution.,Fox RO Jr, Richards FM Nature. 1982 Nov 25;300(5890):325-30. PMID:6292726[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Fox RO Jr, Richards FM. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution. Nature. 1982 Nov 25;300(5890):325-30. PMID:6292726

1amt, resolution 1.50Å

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