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The crystal structure of samarosporin I at atomic resolution

DOI: 10.1002/psc.2454 DOI Help
PMID: 23019149 PMID Help

Authors: Renate Gessmann (IMBB-FORTH) , Danny Axford (Diamond Light Source) , Hans Brückner (University of Giessen; King Saud University) , Kyriacos Petratos (IMBB-FORTH) , Gwyndaf Evans (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Peptide Science , VOL 18 (11) , PAGES 678 - 684

State: Published (Approved)
Published: November 2012

Abstract: 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 310-helical and a minor fraction of ?-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.

Journal Keywords: Crystallography; X-Ray; Hydrogen; Models; Molecular; Peptaibols; Peptides; Sequence Alignment

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography