Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein.

Autor:	Alblova, M.
Další autoři:	Smidova, A. Kalabova, D. Lentini Santo, D. Obšil, Tomáš, 1972- Obšilová, Veronika
Jazyk:	angličtina
Předmět:	vápník konformace enzymy struktura a textura krystalů calcium conformations enzymes crystal structure and texture články journal articles 14-3-3 protein trehalase trehalose allostery
Druh dokumentu:	Non-fiction
ISSN:	0862-8408
Abstrakt:	Abstract: Neutral trehalase 1 (Nth1) from Saccharomyces cerevisiae catalyzes disaccharide trehalose hydrolysis and helps yeast to survive adverse conditions, such as heat shock, starvation or oxidative stress. 14-3-3 proteins, master regulators of hundreds of partner proteins, participate in many key cellular processes. Nth1 is activated by phosphorylation followed by 14-3-3 protein (Bmh) binding. The activation mechanism is also potentiated by Ca2+ binding within the EF-hand-like motif. This review summarizes the current knowledge about trehalases and the molecular and structural basis of Nth1 activation. The crystal structure of fully active Nth1 bound to 14-3-3 protein provided the first high-resolution view of a trehalase from a eukaryotic organism and showed 14-3-3 proteins as structural modulators and allosteric effectors of multi-domain binding partners.
Databáze:	Katalog Knihovny AV ČR
Externí odkaz:	Plný text