1amt: Difference between revisions
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|PDB= 1amt |SIZE=350|CAPTION= <scene name='initialview01'>1amt</scene>, resolution 1.5Å | |PDB= 1amt |SIZE=350|CAPTION= <scene name='initialview01'>1amt</scene>, resolution 1.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1amt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amt OCA], [http://www.ebi.ac.uk/pdbsum/1amt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1amt RCSB]</span> | |||
}} | }} | ||
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[[Category: Fox, R O.]] | [[Category: Fox, R O.]] | ||
[[Category: Richards, F M.]] | [[Category: Richards, F M.]] | ||
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:36 2008'' | ||
Revision as of 18:43, 30 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1AMT is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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