SHORT COMMUNICATION
Hyp-1 protein from St John’s wort as a PR-10 protein
Publication date: 2014-10-23
BioTechnologia 2013;94(1):47-50
ABSTRACT
PR-10 proteins form a large subclass of plant pathogenesis-related proteins that are expressed in response to harmful
environmental factors in a wide range of species. Although their function is still not clear, structural data suggest
that their characteristic internal hydrophobic cavity can bind relevant plant small-molecule mediators. Hyp-1 from
St John's wort (Hypericum perforatum ), initially proposed as a catalyst for the biosynthesis of hypericin, was
eventually shown to share sequence similarity and a folding pattern with PR-10 proteins. The crystal structure of
Hyp-1 in complex with fluorescent probe ANS reveals three distinct and separated binding sites that are unique
among PR-10 proteins. The structure can provide guidance in our quest for the true physiological ligands of Hyp-1.
environmental factors in a wide range of species. Although their function is still not clear, structural data suggest
that their characteristic internal hydrophobic cavity can bind relevant plant small-molecule mediators. Hyp-1 from
St John's wort (Hypericum perforatum ), initially proposed as a catalyst for the biosynthesis of hypericin, was
eventually shown to share sequence similarity and a folding pattern with PR-10 proteins. The crystal structure of
Hyp-1 in complex with fluorescent probe ANS reveals three distinct and separated binding sites that are unique
among PR-10 proteins. The structure can provide guidance in our quest for the true physiological ligands of Hyp-1.
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| eISSN: | 2353-9461 |
| ISSN: | 0860-7796 |
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