1av2: Difference between revisions
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|PDB= 1av2 |SIZE=350|CAPTION= <scene name='initialview01'>1av2</scene>, resolution 1.4Å | |PDB= 1av2 |SIZE=350|CAPTION= <scene name='initialview01'>1av2</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1av2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1av2 OCA], [http://www.ebi.ac.uk/pdbsum/1av2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1av2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Langs, D A.]] | [[Category: Langs, D A.]] | ||
[[Category: Li, N.]] | [[Category: Li, N.]] | ||
[[Category: ion channel]] | [[Category: ion channel]] | ||
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:02 2008'' | ||
Revision as of 15:48, 30 March 2008
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| 1av2, resolution 1.4Å | |||||||||||||
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| Ligands: | CL, CS, DLE, DVA, ETA, FOR, MOH | ||||||||||||
| 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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