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== Structural highlights ==
== Structural highlights ==
<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>
<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='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=MOH:METHANOL'>MOH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tk2|1tk2]], [[2xdc|2xdc]], [[1bdw|1bdw]], [[1c4d|1c4d]], [[1gmk|1gmk]], [[1grm|1grm]], [[1jno|1jno]], [[1kqe|1kqe]], [[1mag|1mag]], [[1mic|1mic]], [[1ng8|1ng8]], [[1nrm|1nrm]], [[1nru|1nru]], [[1nt5|1nt5]], [[1jo3|1jo3]], [[1jo4|1jo4]], [[1nt6|1nt6]], [[1tkq|1tkq]], [[1w5u|1w5u]], [[2izq|2izq]], [[3l8l|3l8l]], [[1al4|1al4]], [[1alx|1alx]], [[1alz|1alz]]</div></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'>[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>
</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.
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>
From MEDLINE&reg;/PubMed&reg;, 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, B M]]
[[Category: Burkhart BM]]
[[Category: Duax, W L]]
[[Category: Duax WL]]
[[Category: Langs, D A]]
[[Category: Langs DA]]
[[Category: Li, N]]
[[Category: Li N]]
[[Category: Antibacterial]]
[[Category: Antibiotic]]
[[Category: Antifungal]]
[[Category: Gramicidin]]
[[Category: Linear gramicidin]]
[[Category: Membrane ion channel]]

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