1av2: Difference between revisions
New page: left|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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[[Image:1av2.gif|left|200px]]<br /><applet load="1av2" size=" | [[Image:1av2.gif|left|200px]]<br /><applet load="1av2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1av2, resolution 1.4Å" /> | caption="1av2, resolution 1.4Å" /> | ||
'''GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER'''<br /> | '''GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
The linear pentadecapeptide antibiotic, gramicidin D, is a naturally | 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== | ==About this Structure== | ||
1AV2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with CS, CL, FOR and MOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1AV2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with <scene name='pdbligand=CS:'>CS</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FOR:'>FOR</scene> and <scene name='pdbligand=MOH:'>MOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Burkhart, B | [[Category: Burkhart, B M.]] | ||
[[Category: Duax, W | [[Category: Duax, W L.]] | ||
[[Category: Langs, D | [[Category: Langs, D A.]] | ||
[[Category: Li, N.]] | [[Category: Li, N.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:33 2008'' | ||
Revision as of 09:48, 21 February 2008
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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 Thu Feb 21 11:48:33 2008
