Four complete turns of a curved 3 10-helix at atomic resolution: The crystal structure of the peptaibol trichovirin I-4A in a polar environment suggests a transition to α-helix for membrane function

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 2, 2012, Pages 109-116

  Gessmann, Renate ^a   Axford, Danny ^b   Owen, Robin L ^b   Brückner, Hans ^c,d   Petratos, Kyriacos ^a  

^a INSTITUTE OF COMPUTER SCIENCE   (Greece)

^b DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^c JUSTUS LIEBIG UNIVERSITY   (Germany)

^d KING SAUD UNIVERSITY   (Saudi Arabia)

Author keywords

peptaibols; peptide antibiotics; transition from 3 10 helix to helix; transmembrane ion channels

Indexed keywords

ANTIINFECTIVE AGENT; FUNGAL PROTEIN; PEPTIDE; TRICHOVIRIN I 4A; TRICHOVIRIN I-4A;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; TRICHODERMA; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; TRICHODERMA;

EID: 84856408778     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S090744491105133X     Document Type: Article

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