This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1av2
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 13: | Line 13: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[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
|
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 , , 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
Page seeded by OCA on Thu Feb 21 11:48:33 2008
Categories: Brevibacillus brevis | Protein complex | Burkhart, B M. | Duax, W L. | Langs, D A. | Li, N. | CL | CS | FOR | MOH | Ion channel | Peptide antibiotic
