1amt
From Proteopedia
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| - | [[Image:1amt.jpg|left|200px]] | + | [[Image:1amt.jpg|left|200px]] |
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| - | '''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1amt |SIZE=350|CAPTION= <scene name='initialview01'>1amt</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AMT is a [ | + | 1AMT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/6292726 6292726] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Fox, R O.]] | [[Category: Fox, R O.]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:46 2008'' |
Revision as of 07:59, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1AMT is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 09:59:46 2008
Categories: Protein complex | Fox, R O. | Richards, F M. | ACE | CCN | MOH | Peptide antibiotic
