| The crystal structure of samarosporin I at atomic resolution. | |
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MedLine Citation:
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PMID: 23019149 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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 α-helical conformation. The helices are significantly bent and packed in an antiparallel fashion in the centered monoclinic lattice leaving among them an approximately 10-Å 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 © 2012 European Peptide Society and John Wiley & Sons, Ltd. |
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Authors:
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Renate Gessmann; Danny Axford; Gwyndaf Evans; Hans Brückner; Kyriacos Petratos |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-9-28 |
Journal Detail:
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Title: Journal of peptide science : an official publication of the European Peptide Society Volume: - ISSN: 1099-1387 ISO Abbreviation: J. Pept. Sci. Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-9-28 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9506309 Medline TA: J Pept Sci Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd. |
Affiliation:
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IMBB-FORTH, N. Plastira 100, Heraklion, 70013, Greece. |
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