Work

Hyp-1 protein from St John’s wort as a PR-10 protein

Year: 2014

Type: article

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.

Source: Biotechnologia

DOI: 10.5114/bta.2013.46437

Authors: Joanna Śliwiak, Zbigniew Dauter, Mariusz Jaskolski

Institutions: Institute of Bioorganic Chemistry, Polish Academy of Sciences, Argonne National Laboratory, National Cancer Institute, Adam Mickiewicz University in Poznań

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: diamond

Funder: European Commission

OpenAlex ID: W2147001788