Non-canonical residues
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Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has been determined using proton two-dimensional NMR (2D-NMR) and restrained molecular dynamics calculations. The global fold of gomesin consists in a wellresolved two-stranded antiparallel b sheet connected by a noncanonical b turn.
9p research12 01-06-2013 30 2 Download
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Formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sul-fatases the oxidation of a specific cysteine residue to formylglycine, which is the catalytic residue required for sulfate ester hydrolysis. This post-trans-lational modification occurs in the endoplasmic reticulum (ER), and is an essential step in the biogenesis of this enzyme family.
13p media19 06-03-2013 45 1 Download