Ostreopexin: A hemopexin fold protein from the oyster mushroom, Pleurotus ostreatus

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• 作者：Katja Ota ; Miha Mikelj ; Tadeja Papler ; Adrijana Leonardi ; Igor Kri?aj ; Peter Ma?ek
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2013
• 出版时间：August, 2013
• 年：2013
• 卷：1834
• 期：8
• 页码：1468-1473
• 全文大小：333 K

文摘

Proteins with hemopexin repeats are widespread in viruses, prokaryotes and eukaryotes. We report here for the first time the existence of a protein in fungi with the four-bladed ¦Â-propeller fold that is typical for hemopexin-like proteins. This protein was isolated from the edible basidiomycetous fungus Pleurotus ostreatus and is named ostreopexin. It binds to Ni^2 +-NTA-agarose, and is structurally and functionally very similar to PA2 albumins isolated from legume seeds and the hemopexin fold protein from rice. Like these plant proteins, ostreopexin shows reversible binding to hemin with moderate affinity, but does not bind to polyamines. We suggest that ostreopexin participates in intracellular management of metal (II or III)-chelates.