4g14

<StructureSection load='4g14' size='340' side='right' caption='[[4g14]], [[Resolution|resolution]] 1.09&Aring;' scene=''>

<table><tr><td colspan='2'>[[4g14]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Samarospora_rostrup Samarospora rostrup]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G14 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G14 FirstGlance]. <br>

</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">[[1joh|1joh]], [[1ob4|1ob4]], [[1ob6|1ob6]], [[1ob7|1ob7]], [[4g13|4g13]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g14 OCA], [http://pdbe.org/4g14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g14 RCSB], [http://www.ebi.ac.uk/pdbsum/4g14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g14 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The atomic resolution structures of samarosporin I have been determined at 100 and 293 K. This is the first crystal structure of a natural 15-residue peptaibol. The amino acid sequence in samarosporin I is identical to emerimicin IV and stilbellin I. Samarosporin is a peptide antibiotic produced by the ascomycetous fungus Samarospora rostrup and belongs to peptaibol subfamily 2. The structures at both temperatures are very similar to each other adopting mainly a 3(10) -helical and a minor fraction of alpha-helical conformation. The helices are significantly bent and packed in an antiparallel fashion in the centered monoclinic lattice leaving among them an approximately 10-A channel extending along the crystallographic twofold axis. Only two ordered water molecules per peptide molecule were located in the channel. Comparisons have been carried out with crystal structures of subfamily 2 16-residue peptaibols antiamoebin and cephaibols. The repercussion of the structural analysis of samarosporin on membrane function is discussed. Copyright (c) 2012 European Peptide Society and John Wiley &amp; Sons, Ltd.

The crystal structure of samarosporin I at atomic resolution.,Gessmann R, Axford D, Evans G, Bruckner H, Petratos K J Pept Sci. 2012 Nov;18(11):678-84. doi: 10.1002/psc.2454. Epub 2012 Sep 28. PMID:23019149<ref>PMID:23019149</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4g14" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Axford, D]]

[[Category: Gessmann, R]]

[[Category: Petratos, K]]

[[Category: Peptaibol]]