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Front Cover: Sphaericin, a Lasso Peptide from the Rare Actinomycete Planomonospora sphaerica (Eur. J. Org. Chem. 8/2017)
Author(s) -
Kodani Shinya,
Inoue Yuto,
Suzuki Masahiro,
Dohra Hideo,
Suzuki Tomohiro,
Hemmi Hikaru,
OhnishiKameyama Mayumi
Publication year - 2017
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201700191
Subject(s) - chemistry , peptide , lasso (programming language) , uniqueness , ring (chemistry) , front cover , stereochemistry , cover (algebra) , crystallography , biochemistry , mathematics , organic chemistry , computer science , mechanical engineering , mathematical analysis , world wide web , engineering
The cover picture shows the three‐dimensional solution structure of a new lasso peptide sphaericin. Lasso peptides are a class of natural occurring peptides, which possess an isopeptide bond and a common knot structural motif. The uniqueness of a lasso peptide is the three‐dimensional structure with a tail part that forms a loop through its own ring. A new lasso peptide named sphaericin was isolated as an antibacterial principle from the rare actinomycete Planomonospora sphaerica . Calculations based on NOE experiments revealed that sphaericin possesses a typical lasso‐peptide fold with a ring, a loop, and a tail. Details are discussed in the Full Paper by S. Kodani et al. on page 1177 ff (DOI: 10.1002/ejoc.201601334 ).