5G5C

Structure of the Pyrococcus furiosus Esterase Pf2001 with space group C2221

Summary for 5G5C

• Entry DOI: 10.2210/pdb5g5c/pdb
• Related: 5G59 5G5M
• Descriptor: ESTERASE (2 entities in total)
• Functional Keywords: structural protein, esterase, themophilic
• Biological source: PYROCOCCUS FURIOSUS
• Total number of polymer chains: 1
• Total formula weight: 31763.53

Authors

Varejao, N.,Reverter, D. (deposition date: 2016-05-23, release date: 2017-06-21, Last modification date: 2024-01-10)

Primary citation

Varejao, N.,De-Andrade, R.A.,Almeida, R.V.,Anobom, C.D.,Foguel, D.,Reverter, D.
Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.
Structure, 26:199-208.e3, 2018

PubMed 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°C and 80°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.

PubMed: 29307486
DOI: 10.1016/j.str.2017.12.004

Experimental method

X-RAY DIFFRACTION (1.18 Å)