Varejao_2018_Structure_26_199

Reference

Title : Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase - Varejao_2018_Structure_26_199
Author(s) : Varejao N , De-Andrade RA , Almeida RV , Anobom CD , Foguel D , Reverter D
Ref : Structure , 26 :199 , 2018
Abstract :

Lipases and esterases constitute a group of enzymes that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from Pyrococcus furiosus reaches its optimal activity between 70 degrees C and 80 degrees C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. The structures reveal important rearrangements in the "cap" subdomain between monomer and dimer, by the formation of an extensive intertwined helical interface. Moreover, the dimer interface is essential for the formation of the hydrophobic channel for substrate selectivity, as confirmed by mutagenesis and kinetic analysis. We also provide evidence for dimer formation at high temperatures, a process that correlates with its enzymatic activation. Thus, we propose a temperature-dependent activation mechanism of the Pf2001 esterase via dimerization that is necessary for the substrate channel formation in the active-site cleft.

PubMedSearch : Varejao_2018_Structure_26_199
PubMedID: 29307486
Gene_locus related to this paper: pyrfu-PF2001

Related information

Inhibitor Pentaethylene-glycol
Gene_locus Pentaethylene-glycol    pyrfu-PF2001
Structure Pentaethylene-glycol    pyrfu-PF2001    5LCN    5G5M    5G59    5G5C

Citations formats

Varejao N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D (2018)
Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase
Structure 26 :199

Varejao N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D (2018)
Structure 26 :199