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Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase
Author(s) -
Kadek Alan,
Kavan Daniel,
Felice Alfons K.G.,
Ludwig Roland,
Halada Petr,
Man Petr
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.03.029
Subject(s) - cellobiose dehydrogenase , divalent , electron transfer , cellobiose , chemistry , ion , calcium , biophysics , dehydrogenase , crystallography , chemical physics , biochemistry , enzyme , photochemistry , biology , organic chemistry , cellulase
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.