1av2
From Proteopedia
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| , resolution 1.4Å | |||||||
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| Ligands: | , , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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