3UF9

Crystal structure of SsoPox in complex with the phosphotriester fensulfothion

Summary for 3UF9

• Entry DOI: 10.2210/pdb3uf9/pdb
• Related: 2VC5 2VC7
• Descriptor: Aryldialkylphosphatase, FE (II) ION, COBALT (II) ION, ... (6 entities in total)
• Functional Keywords: (beta/alpha)8-hydrolase, lactonase, hydrolase
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 4
• Total formula weight: 144600.43

Authors

Elias, M.,Gotthard, G.,Hiblot, J.,Chabriere, E. (deposition date: 2011-10-31, release date: 2012-10-03, Last modification date: 2023-12-06)

Primary citation

Hiblot, J.,Gotthard, G.,Chabriere, E.,Elias, M.
Characterisation of the organophosphate hydrolase catalytic activity of SsoPox
Sci Rep, 2:779-779, 2012

PubMed Abstract: SsoPox is a lactonase endowed with promiscuous phosphotriesterase activity isolated from Sulfolobus solfataricus that belongs to the Phosphotriesterase-Like Lactonase family. Because of its intrinsic thermal stability, SsoPox is seen as an appealing candidate as a bioscavenger for organophosphorus compounds. A comprehensive kinetic characterisation of SsoPox has been performed with various phosphotriesters (insecticides) and phosphodiesters (nerve agent analogues) as substrates. We show that SsoPox is active for a broad range of OPs and remains active under denaturing conditions. In addition, its OP hydrolase activity is highly stimulated by anionic detergent at ambient temperature and exhibits catalytic efficiencies as high as k(cat)/K(M) of 10(5) M(-1)s(-1) against a nerve agent analogue. The structure of SsoPox bound to the phosphotriester fensulfothion reveals an unexpected and non-productive binding mode. This feature suggests that SsoPox's active site is sub-optimal for phosphotriester binding, which depends not only upon shape but also on localised charge of the ligand.

PubMed: 23139857
DOI: 10.1038/srep00779

Experimental method

X-RAY DIFFRACTION (2.68 Å)