1av2: Difference between revisions
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[[Image:1av2.gif|left|200px]] | [[Image:1av2.gif|left|200px]] | ||
'''GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER''' | {{Structure | ||
|PDB= 1av2 |SIZE=350|CAPTION= <scene name='initialview01'>1av2</scene>, resolution 1.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AV2 is a [ | 1AV2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9789021 9789021] | ||
[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:37 2008'' | ||
Revision as of 08:02, 20 March 2008
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| 1av2, resolution 1.4Å | |||||||||||||
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| Ligands: | CS, CL, FOR and MOH | ||||||||||||
| 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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