1ob4: Difference between revisions
New page: left|200px<br /><applet load="1ob4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ob4, resolution 0.95Å" /> '''CEPHAIBOL A'''<br />... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ob4.jpg|left|200px]]<br /><applet load="1ob4" size=" | [[Image:1ob4.jpg|left|200px]]<br /><applet load="1ob4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ob4, resolution 0.95Å" /> | caption="1ob4, resolution 0.95Å" /> | ||
'''CEPHAIBOL A'''<br /> | '''CEPHAIBOL A'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structures of the peptaibol antibiotics cephaibol A, cephaibol | 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== | ==About this Structure== | ||
1OB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acremonium_tubakii Acremonium tubakii] with ACE and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1OB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acremonium_tubakii Acremonium tubakii] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB4 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Bunkoczi, G.]] | [[Category: Bunkoczi, G.]] | ||
[[Category: Schiell, M.]] | [[Category: Schiell, M.]] | ||
[[Category: Sheldrick, G | [[Category: Sheldrick, G M.]] | ||
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
| Line 24: | Line 24: | ||
[[Category: peptaibol]] | [[Category: peptaibol]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:37 2008'' | ||
Revision as of 15:15, 21 February 2008
|
CEPHAIBOL A
OverviewOverview
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 StructureAbout this Structure
1OB4 is a Single protein structure of sequence from Acremonium tubakii with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 14:15:37 2008