1amt: Difference between revisions

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New page: left|200px<br /><applet load="1amt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1amt, resolution 1.5Å" /> '''A VOLTAGE-GATED ION C...
 
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[[Image:1amt.jpg|left|200px]]<br /><applet load="1amt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1amt, resolution 1.5&Aring;" />
'''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION'''<br />


==Overview==
==Crystal structure of alamethicin at 1.5 angstrom resolution==
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.
<StructureSection load='1amt' size='340' side='right'caption='[[1amt]], [[Resolution|resolution]] 1.50&Aring;' 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.


==About this Structure==
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>
1AMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE, CCN and MOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=6292726 6292726]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1amt" style="background-color:#fffaf0;"></div>
[[Category: Fox, R.O.]]
== References ==
[[Category: Richards, F.M.]]
<references/>
[[Category: ACE]]
__TOC__
[[Category: CCN]]
</StructureSection>
[[Category: MOH]]
[[Category: Large Structures]]
[[Category: peptide antibiotic]]
[[Category: Trichoderma viride]]
 
[[Category: Fox RO]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:05:20 2007''
[[Category: Richards FM]]

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

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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