1ob4: Difference between revisions
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|PDB= 1ob4 |SIZE=350|CAPTION= <scene name='initialview01'>1ob4</scene>, resolution 0.95Å | |PDB= 1ob4 |SIZE=350|CAPTION= <scene name='initialview01'>1ob4</scene>, resolution 0.95Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=DIV:D-ISOVALINE'>DIV</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ob4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ob4 OCA], [http://www.ebi.ac.uk/pdbsum/1ob4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ob4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
[[Category: cephaibol]] | [[Category: cephaibol]] | ||
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[[Category: peptaibol]] | [[Category: peptaibol]] | ||
''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 22:42:36 2008'' | ||
Revision as of 19:42, 30 March 2008
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| 1ob4, resolution 0.95Å | |||||||||||||
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| Ligands: | ACE, AIB, DIV, EOH, HYP, PHL | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CEPHAIBOL A
Overview
The crystal structures of the peptaibol antibiotics cephaibol A, cephaibol B and cephaibol C have been determined at ca. 0.9 A resolution. All three adopt a helical conformation with a sharp bend (of about 55 degrees) at the central hydroxyproline. All isovalines were found to possess the D configuration, superposition of all four models (there are two independent molecules in the cephaibol B structure) shows that the N-terminal helix is rigid and the C-terminus is flexible. There are differences in the hydrogen bonding patterns for the three structures that crystallize in different space groups despite relatively similar unit cell dimensions, but only in the case of cephaibol C does the packing emulate the formation of a membrane channel believed to be important for their biological function.
About this Structure
1OB4 is a Single protein structure of sequence from Acremonium tubakii. Full crystallographic information is available from OCA.
Reference
Crystal structures of cephaibols., Bunkoczi G, Schiell M, Vertesy L, Sheldrick GM, J Pept Sci. 2003 Nov-Dec;9(11-12):745-52. PMID:14658793
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