Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2MN5

NMR structure of Copsin

2MN5 の概要
エントリーDOI10.2210/pdb2mn5/pdb
NMR情報BMRB: 19880
分子名称Copsin (1 entity in total)
機能のキーワードantibiotic and antimicrobial protein, antimicrobial protein
由来する生物種Coprinopsis cinerea
タンパク質・核酸の鎖数1
化学式量合計6085.07
構造登録者
Hofmann, D.,Wider, G.,Essig, A.,Aebi, M. (登録日: 2014-03-28, 公開日: 2014-10-29, 最終更新日: 2024-11-06)
主引用文献Essig, A.,Hofmann, D.,Munch, D.,Gayathri, S.,Kunzler, M.,Kallio, P.T.,Sahl, H.G.,Wider, G.,Schneider, T.,Aebi, M.
Copsin, a Novel Peptide-based Fungal Antibiotic Interfering with the Peptidoglycan Synthesis.
J.Biol.Chem., 289:34953-34964, 2014
Cited by
PubMed Abstract: Fungi and bacteria compete with an arsenal of secreted molecules for their ecological niche. This repertoire represents a rich and inexhaustible source for antibiotics and fungicides. Antimicrobial peptides are an emerging class of fungal defense molecules that are promising candidates for pharmaceutical applications. Based on a co-cultivation system, we studied the interaction of the coprophilous basidiomycete Coprinopsis cinerea with different bacterial species and identified a novel defensin, copsin. The polypeptide was recombinantly produced in Pichia pastoris, and the three-dimensional structure was solved by NMR. The cysteine stabilized α/β-fold with a unique disulfide connectivity, and an N-terminal pyroglutamate rendered copsin extremely stable against high temperatures and protease digestion. Copsin was bactericidal against a diversity of Gram-positive bacteria, including human pathogens such as Enterococcus faecium and Listeria monocytogenes. Characterization of the antibacterial activity revealed that copsin bound specifically to the peptidoglycan precursor lipid II and therefore interfered with the cell wall biosynthesis. In particular, and unlike lantibiotics and other defensins, the third position of the lipid II pentapeptide is essential for effective copsin binding. The unique structural properties of copsin make it a possible scaffold for new antibiotics.
PubMed: 25342741
DOI: 10.1074/jbc.M114.599878
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mn5
検証レポート(詳細版)ダウンロードをダウンロード

248942

件を2026-02-11に公開中

PDB statisticsPDBj update infoContact PDBjnumon