1av2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 8: Line 8:
<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>

Latest revision as of 08:55, 3 April 2024

Gramicidin A/CsCl complex, active as a dimerGramicidin A/CsCl complex, active as a dimer

Structural highlights

1av2 is a 4 chain structure with sequence from Brevibacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

1av2, resolution 1.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1av2&oldid=4117746"