4G13
Crystal structure of samarosporin I at 100K
Summary for 4G13
| Entry DOI | 10.2210/pdb4g13/pdb |
| Related | 1JOH 1OB4 1OB6 1OB7 4G14 |
| Related PRD ID | PRD_000920 |
| Descriptor | SAMAROSPORIN I (2 entities in total) |
| Functional Keywords | peptaibol, 3(10)-alpha helix, antibiotic peptide, membrane, extracellular, antibiotic |
| Biological source | samarospora rostrup |
| Total number of polymer chains | 1 |
| Total formula weight | 1557.88 |
| Authors | Gessmann, R.,Axford, D.,Petratos, K. (deposition date: 2012-07-10, release date: 2012-10-03, Last modification date: 2025-03-26) |
| Primary citation | Gessmann, R.,Axford, D.,Evans, G.,Bruckner, H.,Petratos, K. The crystal structure of samarosporin I at atomic resolution. J.Pept.Sci., 18:678-684, 2012 Cited by PubMed 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 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. PubMed: 23019149DOI: 10.1002/psc.2454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.8 Å) |
Structure validation
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