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< | ==Crystal structure of alamethicin at 1.5 angstrom resolution== | ||
<StructureSection load='1amt' size='340' side='right'caption='[[1amt]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1amt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_viride Trichoderma viride]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AMT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=PRD_000163:Alamethicin'>PRD_000163</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1amt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amt OCA], [https://pdbe.org/1amt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1amt RCSB], [https://www.ebi.ac.uk/pdbsum/1amt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1amt ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:6292726</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1amt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Trichoderma viride]] | |||
[[Category: Fox RO]] | |||
== | [[Category: Richards FM]] | ||
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Latest revision as of 13:48, 15 February 2023
Crystal structure of alamethicin at 1.5 angstrom resolutionCrystal structure of alamethicin at 1.5 angstrom resolution
Structural highlights
Publication Abstract from PubMedThe 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 |
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