The disulphide beta-cross: from cystine geometry and clustering to classification of small disulphide-rich protein folds

Journal of Molecular Biology
P M Harrison, M J Sternberg

Abstract

Small disulphide-rich protein folds (SDFs) tend to have less, regular secondary structure than larger protein folds and are thus problematic in protein structure taxonomy and prediction. We report regularities for disulphide-bridged beta-sheet and for cystine clustering that are particularly relevant to such proteins. The repertoire of cystine conformations results in preferences in disulphide distribution between/within beta-sheets. For example, disulphides seldom bridge between beta-sheets with antiparallel orientation for the flanking polypeptide segments, as the separations between packed sheets are such that the only rotamers that straddle them easily are those that generally require parallel orientation. A left-handed chirality preference is described for the intervening connection for disulphides bridging between berta-strands in different sheets in such a parallel orientation. Geometrical analysis of clusters of two cystine residues has shown that closely clustered cystine residues tend to have approximately orthogonal relative orientation. A positive orientation of this type is most often accommodated by a recurrent motif of disulphide-bridged beta-sheet that we call the disulphide beta-cross. The consensus features of...Continue Reading

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