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1av2
From Proteopedia
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(New page: 200px<br /><applet load="1av2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1av2, resolution 1.4Å" /> '''GRAMICIDIN A/CSCL COM...)
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Revision as of 21:14, 24 November 2007
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GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER
Overview
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.
About this Structure
1AV2 is a Protein complex structure of sequences from Brevibacillus brevis with CS, CL, FOR and MOH as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sat Nov 24 23:22:13 2007
Categories: Brevibacillus brevis | Protein complex | Burkhart, B.M. | Duax, W.L. | Langs, D.A. | Li, N. | CL | CS | FOR | MOH | Ion channel | Peptide antibiotic
