5g5m | pdb_00005g5m

Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P21

spinqualitylabelsall models 5g5m, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g5m is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: QRL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8TZJ1_PYRFU Publication Abstract from PubMed 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. Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.,Varejao N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D Structure. 2017 Dec 28. pii: S0969-2126(17)30403-3. doi:, 10.1016/j.str.2017.12.004. PMID:29307486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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