Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10315377" target="_blank" >RIV/00216208:11310/15:10315377 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00444825

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.febslet.2015.03.029" target="_blank" >http://dx.doi.org/10.1016/j.febslet.2015.03.029</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.febslet.2015.03.029" target="_blank" >10.1016/j.febslet.2015.03.029</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase

Popis výsledku v původním jazyce

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 andits 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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Název v anglickém jazyce

Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase

Popis výsledku anglicky

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 andits 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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

FEBS Letters

ISSN

0014-5793

e-ISSN

—

Svazek periodika

589

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

1194-1199

Kód UT WoS článku

000353833900004

EID výsledku v databázi Scopus

2-s2.0-84936741748