3F4C

Crystal structure of organophosphorus hydrolase from Geobacillus stearothermophilus strain 10, with glycerol bound

Summary for 3F4C

• Entry DOI: 10.2210/pdb3f4c/pdb
• Related: 3F4D
• Descriptor: Organophosphorus hydrolase, COBALT (II) ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: alpha-beta barrel, amidohydrolase, binuclear metal enzyme, glycerol-bound, hydrolase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 2
• Total formula weight: 74972.73

Authors

Hawwa, R.,Aikens, J.,Turner, R.J.,Santarsiero, B.,Mesecar, A. (deposition date: 2008-10-31, release date: 2009-09-15, Last modification date: 2023-11-15)

Primary citation

Hawwa, R.,Aikens, J.,Turner, R.J.,Santarsiero, B.D.,Mesecar, A.D.
Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.
Arch.Biochem.Biophys., 488:109-120, 2009

PubMed Abstract: A new enzyme homologous to phosphotriesterase was identified from the bacterium Geobacillus stearothermophilus (GsP). This enzyme belongs to the amidohydrolase family and possesses the ability to hydrolyze both lactone and organophosphate (OP) compounds, making it a phosphotriesterase-like lactonase (PLL). GsP possesses higher OP-degrading activity than recently characterized PLLs, and it is extremely thermostable. GsP is active up to 100 degrees C with an energy of activation of 8.0 kcal/mol towards ethyl paraoxon, and it can withstand an incubation temperature of 60 degrees C for two days. In an attempt to understand the thermostability of PLLs, the X-ray structure of GsP was determined and compared to those of existing PLLs. Based upon a comparative analysis, a new thermal advantage score and plot was developed and reveals that a number of different factors contribute to the thermostability of PLLs.

PubMed: 19615330
DOI: 10.1016/j.abb.2009.06.005

Experimental method

X-RAY DIFFRACTION (2.07 Å)