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1av2
From Proteopedia
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<StructureSection load='1av2' size='340' side='right'caption='[[1av2]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1av2' size='340' side='right'caption='[[1av2]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1av2]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1av2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AV2 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=PRD_000150:GRAMICIDIN+A'>PRD_000150</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=1av2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1av2 OCA], [https://pdbe.org/1av2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1av2 RCSB], [https://www.ebi.ac.uk/pdbsum/1av2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1av2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The linear pentadecapeptide antibiotic, gramicidin D, is a naturally occurring product of Bacillus brevis known to form ion channels in synthetic and natural membranes. The x-ray crystal structures of the right-handed double-stranded double-helical dimers (DSDH) reported here agree with 15N-NMR and CD data on the functional gramicidin D channel in lipid bilayers. These structures demonstrate single-file ion transfer through the channels. The results also indicate that previous crystal structure reports of a left-handed double-stranded double-helical dimer in complex with Cs+ and K+ salts may be in error and that our evidence points to the DSDH as the major conformer responsible for ion transport in membranes. | ||
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| - | The conducting form of gramicidin A is a right-handed double-stranded double helix.,Burkhart BM, Li N, Langs DA, Pangborn WA, Duax WL Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12950-5. PMID:9789021<ref>PMID:9789021</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1av2" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Gramicidin|Gramicidin]] | *[[Gramicidin|Gramicidin]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Burkhart | + | [[Category: Burkhart BM]] |
| - | [[Category: Duax | + | [[Category: Duax WL]] |
| - | [[Category: Langs | + | [[Category: Langs DA]] |
| - | [[Category: Li | + | [[Category: Li N]] |
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Current revision
Gramicidin A/CsCl complex, active as a dimer
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