1ob7: Difference between revisions
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<StructureSection load='1ob7' size='340' side='right'caption='[[1ob7]], [[Resolution|resolution]] 0.89Å' scene=''> | <StructureSection load='1ob7' size='340' side='right'caption='[[1ob7]], [[Resolution|resolution]] 0.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ob7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ob7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acremonium_tubakii Acremonium tubakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OB7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m24|1m24]], [[1r9u|1r9u]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1gq0|1gq0]], [[1joh|1joh]], [[1amt|1amt]], [[1ee7|1ee7]], [[1ob6|1ob6]], [[1ob4|1ob4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m24|1m24]], [[1r9u|1r9u]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1gq0|1gq0]], [[1joh|1joh]], [[1amt|1amt]], [[1ee7|1ee7]], [[1ob6|1ob6]], [[1ob4|1ob4]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ob7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ob7 OCA], [https://pdbe.org/1ob7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ob7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ob7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ob7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:06, 24 February 2021
Cephaibol CCephaibol C
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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