Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
Odkazy
PubMed
25862501
DOI
10.1016/j.febslet.2015.03.029
PII: S0014-5793(15)00207-0
Knihovny.cz E-zdroje
- Klíčová slova
- Calcium effect, Cellobiose dehydrogenase, Electrostatic interaction, Flavocytochrome, Hydrogen/deuterium exchange, Interdomain electron transfer,
- MeSH
- fungální proteiny chemie MeSH
- karbohydrátdehydrogenasy chemie MeSH
- Sordariales enzymologie MeSH
- terciární struktura proteinů MeSH
- transport elektronů fyziologie MeSH
- vápník chemie MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- cellobiose-quinone oxidoreductase MeSH Prohlížeč
- fungální proteiny MeSH
- karbohydrátdehydrogenasy MeSH
- vápník MeSH
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.
