Cellobiose dehydrogenase (CDH) from wood degrading fungi represents a subclass of oxidoreductases with unique properties. Consisting of two domains exhibiting interdomain electron transfer, this is the only known flavocytochrome involved in wood degradation. High resolution structures of the separated domains were solved, but the overall architecture of the intact protein and the exact interface of the two domains is unknown. Recently, it was shown that divalent cations modulate the activity of CDH and its pH optimum and a possible mechanism involving bridging of negative charges by calcium ions was proposed. Here we provide a structural explanation of this phenomenon confirming the interaction between negatively charged surface patches and calcium ions at the domain interface.

Department of Food Sciences and Technology Food Biotechnology Laboratory BOKU University of Natural Resources and Life Sciences Muthgasse 18 1190 Vienna Austria

Institute of Microbiology The Czech Academy of Sciences Videnska 1083 Prague Czech Republic

Institute of Microbiology The Czech Academy of Sciences Videnska 1083 Prague Czech Republic; Department of Biochemistry Faculty of Science Charles University Prague Hlavova 8 Prague Czech Republic

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