(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > PVC group: NE > Planctomycetes: NE > Planctomycetia: NE > Planctomycetales: NE > Planctomycetaceae: NE > Thermogutta: NE > Thermogutta terrifontis: NE
No mutation 10 structures(e.g. : 5AO9, 5AOA, 5AOB... more)(less) 5AO9: The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-native, 5AOA: The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-Propionate bound, 5AOB: The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound, 5AOC: The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound, 7BFN: Apo form of Thermogutta terrifontis esterase 2, 7BFO: Thermogutta terrifontis esterase 2 phosphonylated by VX, 7BFR: Thermogutta terrifontis esterase 2 phosphorylated by paraoxon, 7BFT: Thermogutta terrifontis esterase 2 phosphoramylated by tabun, 7BFU: Thermogutta terrifontis esterase 2 phosphonylated by sarin, 7BFV: Thermogutta terrifontis esterase 2 phosphonylated by cyclosarin No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA AEVGRLRYPPEMPGAEVKVYKKVDNVDLKLYIYKPADWKPADRRSAIVFF FGGGWQSGSPAQFRPQCEYFAGRGMVAMAADYRVGSRHNVKVADCVADAK SAIRWVRQHAAELGVDPQKIVASGGSAGGHLAACTVMVPDLEAPEEDHTI SSQANAAILFNPVLILSREGLKDHVPRQDWEERLRERLGTEPKAVSPYHH IRAGLPPMIIFHGTADNTVPFETIRLFAEAMKKAGNRCELVPFEGAAHGF FNFGRGDNLAYQKTLELADEFLVEIGFLAPKGESQP
Organophosphorous nerve agents (OPNA) pose an actual and major threat for both military and civilians alike, as an upsurge in their use has been observed in the recent years. Currently available treatments mitigate the effect of the nerve agents, and could be vastly improved by means of scavengers of the nerve agents. Consequently, efforts have been made over the years into investigating enzymes, also known as bioscavengers, which have the potential either to trap or hydrolyze these toxic compounds. We investigated the previously described esterase 2 from Thermogutta terrifontis (TtEst2) as a potential bioscavenger of nerve agents. As such, we assessed its potential against G-agents (tabun, sarin, and cyclosarin), VX, as well as the pesticide paraoxon. We report that TtEst2 is a good bioscavenger of paraoxon and G-agents, but is rather slow at scavenging VX. X-ray crystallography studies showed that TtEst2 forms an irreversible complex with the aforementioned agents, and allowed the identification of amino-acids, whose mutagenesis could lead to better scavenging properties for VX. In conjunction with its cheap production and purification processes, as well as a robust structural backbone, further engineering of TtEst2 could lead to a stopgap bioscavenger useful for in corpo scavenging or skin decontamination.
Title: The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Reveals an Open Active Site Due to a Minimal 'Cap' Domain Sayer C, Szabo Z, Isupov MN, Ingham C, Littlechild JA Ref: Front Microbiol, 6:1294, 2015 : PubMed
A carboxyl esterase (TtEst2) has been identified in a novel thermophilic bacterium, Thermogutta terrifontis from the phylum Planctomycetes and has been cloned and over-expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity toward small p-nitrophenyl (pNP) carboxylic esters with optimal activity for pNP-acetate. The enzyme shows moderate thermostability retaining 75% activity after incubation for 30 min at 70 degrees C. The crystal structures have been determined for the native TtEst2 and its complexes with the carboxylic acid products propionate, butyrate, and valerate. TtEst2 differs from most enzymes of the alpha/beta-hydrolase family 3 as it lacks the majority of the 'cap' domain and its active site cavity is exposed to the solvent. The bound ligands have allowed the identification of the carboxyl pocket in the enzyme active site. Comparison of TtEst2 with structurally related enzymes has given insight into how differences in their substrate preference can be rationalized based upon the properties of their active site pockets.
Thermogutta terrifontis thermophilic esterase with minimal cap domain from a Planctomycetes species
