1bdw
From Proteopedia
(New page: 200px<br /><applet load="1bdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bdw, resolution 1.70Å" /> '''GRAMICIDIN D FROM BA...) |
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| - | [[Image:1bdw.gif|left|200px]]<br /><applet load="1bdw" size=" | + | [[Image:1bdw.gif|left|200px]]<br /><applet load="1bdw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bdw, resolution 1.70Å" /> | caption="1bdw, resolution 1.70Å" /> | ||
'''GRAMICIDIN D FROM BACILLUS BREVIS (ACTIVE FORM)'''<br /> | '''GRAMICIDIN D FROM BACILLUS BREVIS (ACTIVE FORM)'''<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== | ||
| - | 1BDW 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 FOR and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BDW 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=FOR:'>FOR</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDW 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: Pangborn, W | + | [[Category: Pangborn, W A.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: FOR]] | [[Category: FOR]] | ||
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:13 2008'' |
Revision as of 09:54, 21 February 2008
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GRAMICIDIN D FROM BACILLUS BREVIS (ACTIVE FORM)
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
1BDW is a Protein complex structure of sequences from Brevibacillus brevis with and 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
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