This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1amt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 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 C...)
Current revision (10:48, 15 February 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[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]]

Current revision

Crystal structure of alamethicin at 1.5 angstrom resolution

PDB ID 1amt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1amt"
Personal tools